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Conserved domains on  [gi|4505211|ref|NP_002419|]
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matrix metalloproteinase-15 preproprotein [Homo sapiens]

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 ...
 138-304 1.75e-87

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: 270.26  E-value: 1.75e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211    138 KWNNHHLTFSIQNYTEKLGWYHSMEAVRRAFRVWEQATPLVFQEVPYEdirlrrqkEADIMVLFASGFHGDSSPFDGTGG 217
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTG--------EADIMIGFGRGDHGDGYPFDGPGG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211    218 FLAHAYFPGPGLGGDTHFDADEPWTFSSTDLHGNNLFLVAVHELGHALGLEHSSNPNAIMAPFYQWKDVDNFKLPEDDLR 297
Cdd:pfam00413  73 VLAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIK 152


                  ....*..
gi 4505211    298 GIQQLYG 304
Cdd:pfam00413 153 GIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 367-559 1.16e-76

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: 243.37  E-value: 1.16e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211  367 PNICDGD-FDTVAMLRGEMFVFKGRWFWRVRHNRVlDNYPMPIGHFWRGLPGDISAAYER-QDGRFVFFKGDRYWLFREA 444
Cdd:cd00094   1 PDACDPLsFDAVTTLRGELYFFKGRYFWRLSPGKP-PGSPFLISSFWPSLPSPVDAAFERpDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211  445 NLEPGYPQPLTSYGLGIPYDRIDTAIWWEPTGHTFFFQEDRYWRFNEETQRGDPGYPKPIS-VWQGIPASPKGAFLSNDa 523
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIEtDFPGVPDKVDAAFRWLD- 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 4505211  524 AYTYFYKGTKYWKFDNERLRMEPGYPKSILRDFMGC 559
Cdd:cd00094 159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 643-669 7.96e-12

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: 61.18  E-value: 7.96e-12
                          10        20
                  ....*....|....*....|....*..
gi 4505211    643 TYALVQMQRKGAPRVLLYCKRSLQEWV 669
Cdd:pfam11857  46 IYAIVQFQRKGTPRRLLYCKRSLQDWV 72
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 53-106 1.49e-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: 1.49e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 4505211     53 AENWLRLYGYLPQPSrhmsTMRSAQILASALAEMQRFYGIPVTGVLDEETKEWM 106
Cdd:pfam01471   8 LQRYLNRLGYYPGPV----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 ...
 138-304 1.75e-87

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: 270.26  E-value: 1.75e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211    138 KWNNHHLTFSIQNYTEKLGWYHSMEAVRRAFRVWEQATPLVFQEVPYEdirlrrqkEADIMVLFASGFHGDSSPFDGTGG 217
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTG--------EADIMIGFGRGDHGDGYPFDGPGG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211    218 FLAHAYFPGPGLGGDTHFDADEPWTFSSTDLHGNNLFLVAVHELGHALGLEHSSNPNAIMAPFYQWKDVDNFKLPEDDLR 297
Cdd:pfam00413  73 VLAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIK 152


                  ....*..
gi 4505211    298 GIQQLYG 304
Cdd:pfam00413 153 GIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 138-304 5.70e-78

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: 245.58  E-value: 5.70e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211  138 KWNNHHLTFSIQNYTEKLGWYHSMEAVRRAFRVWEQATPLVFQEVPYedirlrrQKEADIMVLFASGFHGDSSPFDGTGG 217
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTS-------GQEADIRISFARGNHGDGYPFDGPGG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211  218 FLAHAYFPGpGLGGDTHFDADEPWTFSSTDlHGNNLFLVAVHELGHALGLEHSSNPNAIMAPFYQWKDVdNFKLPEDDLR 297
Cdd:cd04278  74 TLAHAFFPG-GIGGDIHFDDDEQWTLGSDS-GGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIR 150


                ....*..
gi 4505211  298 GIQQLYG 304
Cdd:cd04278 151 GIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 367-559 1.16e-76

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: 243.37  E-value: 1.16e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211  367 PNICDGD-FDTVAMLRGEMFVFKGRWFWRVRHNRVlDNYPMPIGHFWRGLPGDISAAYER-QDGRFVFFKGDRYWLFREA 444
Cdd:cd00094   1 PDACDPLsFDAVTTLRGELYFFKGRYFWRLSPGKP-PGSPFLISSFWPSLPSPVDAAFERpDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211  445 NLEPGYPQPLTSYGLGIPYDRIDTAIWWEPTGHTFFFQEDRYWRFNEETQRGDPGYPKPIS-VWQGIPASPKGAFLSNDa 523
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIEtDFPGVPDKVDAAFRWLD- 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 4505211  524 AYTYFYKGTKYWKFDNERLRMEPGYPKSILRDFMGC 559
Cdd:cd00094 159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 137-304 6.31e-32

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: 120.53  E-value: 6.31e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211     137 RKWNNHHLTFSIqnYTEKLGWYhSMEAVRRAFRVWEQATPLVFQEVPYEdirlrrqkeADIMVLFASGFHGdsspfdgtg 216
Cdd:smart00235   3 KKWPKGTVPYVI--DSSSLSPE-EREAIAKALAEWSDVTCIRFVERTGT---------ADIYISFGSGDSG--------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211     217 GFLAHAYFPGpglgGDTHFDaDEPWTFSSTdlhgnnlflVAVHELGHALGLEHSSNPNA---IMAPFYQWKDVDNFKLPE 293
Cdd:smart00235  62 CTLSHAGRPG----GDQHLS-LGNGCINTG---------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSE 127

                          170
                   ....*....|.
gi 4505211     294 DDLRGIQQLYG 304
Cdd:smart00235 128 DDSLGIPYDYG 138
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 643-669 7.96e-12

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: 61.18  E-value: 7.96e-12
                          10        20
                  ....*....|....*....|....*..
gi 4505211    643 TYALVQMQRKGAPRVLLYCKRSLQEWV 669
Cdd:pfam11857  46 IYAIVQFQRKGTPRRLLYCKRSLQDWV 72
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 419-462 1.00e-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: 57.25  E-value: 1.00e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 4505211     419 ISAAYERQDGRFVFFKGDRYWLFREANLEPGYPQPLTSYGLGIP 462
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 466-511 2.01e-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: 56.04  E-value: 2.01e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 4505211    466 IDTAIWWEPtGHTFFFQEDRYWRFNEETQrgDPGYPKPISVWQGIP 511
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQRV--EPGYPKLISDFPGLP 43
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 53-106 1.49e-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: 1.49e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 4505211     53 AENWLRLYGYLPQPSrhmsTMRSAQILASALAEMQRFYGIPVTGVLDEETKEWM 106
Cdd:pfam01471   8 LQRYLNRLGYYPGPV----DGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
257-277 8.39e-05

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 43.76  E-value: 8.39e-05
                         10        20
                 ....*....|....*....|.
gi 4505211   257 AVHELGHALGLEHSSNPNAIM 277
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVM 146
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
256-279 3.04e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 41.87  E-value: 3.04e-04
                        10        20
                ....*....|....*....|....
gi 4505211  256 VAVHELGHALGLEHSSNPNAIMAP 279
Cdd:COG1913 126 EAVHELGHLFGLGHCPNPRCVMHF 149
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 257-277 4.66e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 38.46  E-value: 4.66e-03
                         10        20
                 ....*....|....*....|.
gi 4505211   257 AVHELGHALGLEHSSNPNAIM 277
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 ...
 138-304 1.75e-87

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: 270.26  E-value: 1.75e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211    138 KWNNHHLTFSIQNYTEKLGWYHSMEAVRRAFRVWEQATPLVFQEVPYEdirlrrqkEADIMVLFASGFHGDSSPFDGTGG 217
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTG--------EADIMIGFGRGDHGDGYPFDGPGG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211    218 FLAHAYFPGPGLGGDTHFDADEPWTFSSTDLHGNNLFLVAVHELGHALGLEHSSNPNAIMAPFYQWKDVDNFKLPEDDLR 297
Cdd:pfam00413  73 VLAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIK 152


                  ....*..
gi 4505211    298 GIQQLYG 304
Cdd:pfam00413 153 GIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 138-304 5.70e-78

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: 245.58  E-value: 5.70e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211  138 KWNNHHLTFSIQNYTEKLGWYHSMEAVRRAFRVWEQATPLVFQEVPYedirlrrQKEADIMVLFASGFHGDSSPFDGTGG 217
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTS-------GQEADIRISFARGNHGDGYPFDGPGG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211  218 FLAHAYFPGpGLGGDTHFDADEPWTFSSTDlHGNNLFLVAVHELGHALGLEHSSNPNAIMAPFYQWKDVdNFKLPEDDLR 297
Cdd:cd04278  74 TLAHAFFPG-GIGGDIHFDDDEQWTLGSDS-GGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIR 150


                ....*..
gi 4505211  298 GIQQLYG 304
Cdd:cd04278 151 GIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 367-559 1.16e-76

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: 243.37  E-value: 1.16e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211  367 PNICDGD-FDTVAMLRGEMFVFKGRWFWRVRHNRVlDNYPMPIGHFWRGLPGDISAAYER-QDGRFVFFKGDRYWLFREA 444
Cdd:cd00094   1 PDACDPLsFDAVTTLRGELYFFKGRYFWRLSPGKP-PGSPFLISSFWPSLPSPVDAAFERpDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211  445 NLEPGYPQPLTSYGLGIPYDRIDTAIWWEPTGHTFFFQEDRYWRFNEETQRGDPGYPKPIS-VWQGIPASPKGAFLSNDa 523
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIEtDFPGVPDKVDAAFRWLD- 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 4505211  524 AYTYFYKGTKYWKFDNERLRMEPGYPKSILRDFMGC 559
Cdd:cd00094 159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 137-304 6.31e-32

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: 120.53  E-value: 6.31e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211     137 RKWNNHHLTFSIqnYTEKLGWYhSMEAVRRAFRVWEQATPLVFQEVPYEdirlrrqkeADIMVLFASGFHGdsspfdgtg 216
Cdd:smart00235   3 KKWPKGTVPYVI--DSSSLSPE-EREAIAKALAEWSDVTCIRFVERTGT---------ADIYISFGSGDSG--------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211     217 GFLAHAYFPGpglgGDTHFDaDEPWTFSSTdlhgnnlflVAVHELGHALGLEHSSNPNA---IMAPFYQWKDVDNFKLPE 293
Cdd:smart00235  62 CTLSHAGRPG----GDQHLS-LGNGCINTG---------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSE 127

                          170
                   ....*....|.
gi 4505211     294 DDLRGIQQLYG 304
Cdd:smart00235 128 DDSLGIPYDYG 138
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 157-304 8.91e-16

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: 75.19  E-value: 8.91e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211  157 WYHSM-EAVRRAFRVWEQATPLVFQEVPyedirlRRQKEADIMVLFasgfhGDSSPFDGTGGFLAHAYFPGPGLGGDT-- 233
Cdd:cd04279  18 RAQSWlQAVKQAAAEWENVGPLKFVYNP------EEDNDADIVIFF-----DRPPPVGGAGGGLARAGFPLISDGNRKlf 86

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4505211  234 -HFDADEPWTFSSTDLhgnNLFLVAVHELGHALGLEHSS-NPNAIMAPFYQWKDVDNFKLPEDDLRGIQQLYG 304
Cdd:cd04279  87 nRTDINLGPGQPRGAE---NLQAIALHELGHALGLWHHSdRPEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 162-304 2.03e-14

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: 72.06  E-value: 2.03e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211  162 EAVRRAFRVWEQATPLVFQEVPYEDirlrrqkEADIMvlfasgFHGDSSPFDGTGGFlahAYFPGPG----LGGDTHFDA 237
Cdd:cd04277  37 AAARDALEAWEDVADIDFVEVSDNS-------GADIR------FGNSSDPDGNTAGY---AYYPGSGsgtaYGGDIWFNS 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211  238 DEPWTFSSTdlhGNNLFLVAVHELGHALGLEHS-----SNPNAIMAPFYQWKD-------------VDNFKLPE----DD 295
Cdd:cd04277 101 SYDTNSDSP---GSYGYQTIIHEIGHALGLEHPgdyngGDPVPPTYALDSREYtvmsynsgygngaSAGGGYPQtpmlLD 177


                ....*....
gi 4505211  296 LRGIQQLYG 304
Cdd:cd04277 178 IAALQYLYG 186
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 643-669 7.96e-12

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: 61.18  E-value: 7.96e-12
                          10        20
                  ....*....|....*....|....*..
gi 4505211    643 TYALVQMQRKGAPRVLLYCKRSLQEWV 669
Cdd:pfam11857  46 IYAIVQFQRKGTPRRLLYCKRSLQDWV 72
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 162-303 2.09e-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: 2.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211  162 EAVRRAFRVWEQATPLVFQEVPYEDIRlrrqkeADIMVLFASGfhgdsspfDGTGGFLAHAYFPG--PGLGGDTHFDADE 239
Cdd:cd00203  25 SLILIAMQIWRDYLNIRFVLVGVEIDK------ADIAILVTRQ--------DFDGGTGGWAYLGRvcDSLRGVGVLQDNQ 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211  240 PWTFsstdlhgnNLFLVAVHELGHALGLEHSSNPNA--------------------IMAPFY-QWKDVDNFKLPEDDLRG 298
Cdd:cd00203  91 SGTK--------EGAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKgSFSDGQRKDFSQCDIDQ 162


                ....*
gi 4505211  299 IQQLY 303
Cdd:cd00203 163 INKLY 167
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 419-462 1.00e-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: 57.25  E-value: 1.00e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 4505211     419 ISAAYERQDGRFVFFKGDRYWLFREANLEPGYPQPLTSYGLGIP 462
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 466-511 2.01e-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: 56.04  E-value: 2.01e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 4505211    466 IDTAIWWEPtGHTFFFQEDRYWRFNEETQrgDPGYPKPISVWQGIP 511
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQRV--EPGYPKLISDFPGLP 43
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 419-462 2.10e-09

Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 53.34  E-value: 2.10e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 4505211    419 ISAAYERQDGRFVFFKGDRYWLFREANLEPGYPQPLTSYgLGIP 462
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKLISDF-PGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 466-511 8.96e-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: 51.47  E-value: 8.96e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 4505211     466 IDTAIWWEPtGHTFFFQEDRYWRFNEetQRGDPGYPKPIS-VWQGIP 511
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDP--KRVDPGYPKLISsFFPGLP 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 53-106 1.49e-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: 1.49e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 4505211     53 AENWLRLYGYLPQPSrhmsTMRSAQILASALAEMQRFYGIPVTGVLDEETKEWM 106
Cdd:pfam01471   8 LQRYLNRLGYYPGPV----DGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 162-271 3.09e-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: 53.65  E-value: 3.09e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211  162 EAVRRAFRVWEQATPLVFQEVpyedirlRRQKEADIMVlfasGFHGDSSPFDGTGGFLAHAYFPGPGlggdTHFDADEPW 241
Cdd:cd04268  18 AAILDAIEAWNKAFAIGFKNA-------NDVDPADIRY----SVIRWIPYNDGTWSYGPSQVDPLTG----EILLARVYL 82

                        90       100       110
                ....*....|....*....|....*....|
gi 4505211  242 TFSSTDLHGNNLFLVAVHELGHALGLEHSS 271
Cdd:cd04268  83 YSSFVEYSGARLRNTAEHELGHALGLRHNF 112
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 374-416 6.80e-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: 49.10  E-value: 6.80e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 4505211    374 FDTVAMLR-GEMFVFKGRWFWRVRHNRVLDNYPMPIGHFwRGLP 416
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVEPGYPKLISDF-PGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 522-558 2.74e-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: 2.74e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 4505211     522 DAAY------TYFYKGTKYWKFDNErlRMEPGYPKSILRDFMG 558
Cdd:smart00120   2 DAAFelrdgkTYFFKGDKYWRFDPK--RVDPGYPKLISSFFPG 42
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 522-559 9.79e-07

Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 45.64  E-value: 9.79e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 4505211    522 DAAY------TYFYKGTKYWKFDNErlRMEPGYPKSILRD-FMGC 559
Cdd:pfam00045   2 DAAFedrdgkTYFFKGRKYWRFDPQ--RVEPGYPKLISDFpGLPC 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 374-417 9.79e-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: 45.70  E-value: 9.79e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 4505211     374 FDTVAMLR-GEMFVFKGRWFWRVRHNRVLDNYPMPIGHFWRGLPG 417
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
257-277 8.39e-05

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 43.76  E-value: 8.39e-05
                         10        20
                 ....*....|....*....|.
gi 4505211   257 AVHELGHALGLEHSSNPNAIM 277
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVM 146
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
256-279 3.04e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 41.87  E-value: 3.04e-04
                        10        20
                ....*....|....*....|....
gi 4505211  256 VAVHELGHALGLEHSSNPNAIMAP 279
Cdd:COG1913 126 EAVHELGHLFGLGHCPNPRCVMHF 149
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 256-279 1.47e-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: 39.97  E-value: 1.47e-03
                        10        20
                ....*....|....*....|....
gi 4505211  256 VAVHELGHALGLEHSSNPNAIMAP 279
Cdd:cd11375 126 EAVHELGHLFGLDHCPYYACVMNF 149
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 162-269 1.49e-03

Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239819 [Multi-domain]  Cd Length: 198  Bit Score: 40.44  E-value: 1.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211  162 EAVRRAFRVWEQATPLVFQEVPYEDirlrrqkeADIMVLFASGfHGDSSpFDGTGGFLAHAYFPGPGLGGDTHFDADEpw 241
Cdd:cd04327  23 DKVRAAAREWLPYANLKFKFVTDAD--------ADIRISFTPG-DGYWS-YVGTDALLIGADAPTMNLGWFTDDTPDP-- 90

                        90       100
                ....*....|....*....|....*...
gi 4505211  242 TFSSTdlhgnnlflvAVHELGHALGLEH 269
Cdd:cd04327  91 EFSRV----------VLHEFGHALGFIH 108
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 162-279 3.63e-03

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 39.67  E-value: 3.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505211  162 EAVRRAFRVWEQATPLvfQEVpyedirlrRQKE-ADIMVLFAS---GFHGDSSP----------FDGTGGFLAHayfpgp 227
Cdd:COG5549 104 AAVLQAIAEWNAYLPL--EVV--------ENPEnADIIIVRSNpplTASPNPETgarsaettyeFYDTGNILSH------ 167

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4505211  228 glggdthfdadepwTFS---STDLHGNNLFLVAVHELGHALGLE-HSSNPNAIMAP 279
Cdd:COG5549 168 --------------RFTillSPNQTGKYLLATARHELGHALGIWgHSPSPTDAMYF 209
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 257-277 4.66e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 38.46  E-value: 4.66e-03
                         10        20
                 ....*....|....*....|.
gi 4505211   257 AVHELGHALGLEHSSNPNAIM 277
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVM 149
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 249-280 4.73e-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: 4.73e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 4505211  249 HGNNLFLVAV---HELGHALGLEHS------SNPNAIMAPF 280
Cdd:cd04269 124 HSRNLLLFAVtmaHELGHNLGMEHDdggctcGRSTCIMAPS 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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