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Conserved domains on  [gi|1622914373|ref|XP_001101050|]
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matrix metalloproteinase-15 [Macaca mulatta]

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 2.07e-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: 2.07e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373 138 KWNNHHLTFSIQNYTEKLGWYHSMEAVRRAFRVWEQATPLVFQEVPYEdirlrrqkEADIMVLFASGFHGDSSPFDGTGG 217
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTG--------EADIMIGFGRGDHGDGYPFDGPGG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373 218 FLAHAYFPGPGLGGDTHFDADEPWTFSSTDLHGNNLFLVAVHELGHALGLEHSSNPNAIMAPFYQWKDVDNFKLPEDDLR 297
Cdd:pfam00413  73 VLAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIK 152


                  ....*..
gi 1622914373 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 3.49e-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: 242.22  E-value: 3.49e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373 367 PNICDGD-FDTVAMLRGEMFVFKGRWFWRVRHNRVlDNYPMPIGHFWRGLPSDISAAYER-QDGRFVFFKGDRYWLFREA 444
Cdd:cd00094     1 PDACDPLsFDAVTTLRGELYFFKGRYFWRLSPGKP-PGSPFLISSFWPSLPSPVDAAFERpDTGKIYFFKGDKYWVYTGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373 445 NLEPGYPQPLTSYGLGIPYDRIDTAIWWEPTGHTFFFQEDRYWRFNEETQRGDPGYPKSIS-IWQGIPASPKGAFLSNDa 523
Cdd:cd00094    80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIEtDFPGVPDKVDAAFRWLD- 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622914373 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 1622914373 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 1.36e-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: 1.36e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622914373  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 2.07e-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: 2.07e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373 138 KWNNHHLTFSIQNYTEKLGWYHSMEAVRRAFRVWEQATPLVFQEVPYEdirlrrqkEADIMVLFASGFHGDSSPFDGTGG 217
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTG--------EADIMIGFGRGDHGDGYPFDGPGG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373 218 FLAHAYFPGPGLGGDTHFDADEPWTFSSTDLHGNNLFLVAVHELGHALGLEHSSNPNAIMAPFYQWKDVDNFKLPEDDLR 297
Cdd:pfam00413  73 VLAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIK 152


                  ....*..
gi 1622914373 298 GIQQLYG 304
Cdd:pfam00413 153 GIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 138-304 6.69e-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: 245.19  E-value: 6.69e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373 138 KWNNHHLTFSIQNYTEKLGWYHSMEAVRRAFRVWEQATPLVFQEVPYedirlrrQKEADIMVLFASGFHGDSSPFDGTGG 217
Cdd:cd04278     1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTS-------GQEADIRISFARGNHGDGYPFDGPGG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373 218 FLAHAYFPGpGLGGDTHFDADEPWTFSSTDlHGNNLFLVAVHELGHALGLEHSSNPNAIMAPFYQWKDVdNFKLPEDDLR 297
Cdd:cd04278    74 TLAHAFFPG-GIGGDIHFDDDEQWTLGSDS-GGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIR 150


                  ....*..
gi 1622914373 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 3.49e-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: 242.22  E-value: 3.49e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373 367 PNICDGD-FDTVAMLRGEMFVFKGRWFWRVRHNRVlDNYPMPIGHFWRGLPSDISAAYER-QDGRFVFFKGDRYWLFREA 444
Cdd:cd00094     1 PDACDPLsFDAVTTLRGELYFFKGRYFWRLSPGKP-PGSPFLISSFWPSLPSPVDAAFERpDTGKIYFFKGDKYWVYTGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373 445 NLEPGYPQPLTSYGLGIPYDRIDTAIWWEPTGHTFFFQEDRYWRFNEETQRGDPGYPKSIS-IWQGIPASPKGAFLSNDa 523
Cdd:cd00094    80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIEtDFPGVPDKVDAAFRWLD- 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622914373 524 AYTYFYKGTKYWKFDNERLRMEPGYPKSILRDFMGC 559
Cdd:cd00094   159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 137-304 1.06e-31

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: 120.15  E-value: 1.06e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373  137 RKWNNHHLTFSIqnYTEKLGWYhSMEAVRRAFRVWEQATPLVFQEVPYEdirlrrqkeADIMVLFASGFHGdsspfdgtg 216
Cdd:smart00235   3 KKWPKGTVPYVI--DSSSLSPE-EREAIAKALAEWSDVTCIRFVERTGT---------ADIYISFGSGDSG--------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373  217 GFLAHAYFPGpglgGDTHFDaDEPWTFSSTdlhgnnlflVAVHELGHALGLEHSSNPNA---IMAPFYQWKDVDNFKLPE 293
Cdd:smart00235  62 CTLSHAGRPG----GDQHLS-LGNGCINTG---------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSE 127

                          170
                   ....*....|.
gi 1622914373  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 1622914373 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 9.02e-11

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: 9.02e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1622914373  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 1.52e-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: 1.52e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1622914373 466 IDTAIWWEPtGHTFFFQEDRYWRFNEETQrgDPGYPKSISIWQGIP 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 1.36e-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: 1.36e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622914373  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 1622914373 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 1622914373 256 VAVHELGHALGLEHSSNPNAIMAP 279
Cdd:COG1913   126 EAVHELGHLFGLGHCPNPRCVMHF 149
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 257-277 4.41e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 38.85  E-value: 4.41e-03
                          10        20
                  ....*....|....*....|.
gi 1622914373 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 2.07e-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: 2.07e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373 138 KWNNHHLTFSIQNYTEKLGWYHSMEAVRRAFRVWEQATPLVFQEVPYEdirlrrqkEADIMVLFASGFHGDSSPFDGTGG 217
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTG--------EADIMIGFGRGDHGDGYPFDGPGG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373 218 FLAHAYFPGPGLGGDTHFDADEPWTFSSTDLHGNNLFLVAVHELGHALGLEHSSNPNAIMAPFYQWKDVDNFKLPEDDLR 297
Cdd:pfam00413  73 VLAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIK 152


                  ....*..
gi 1622914373 298 GIQQLYG 304
Cdd:pfam00413 153 GIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 138-304 6.69e-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: 245.19  E-value: 6.69e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373 138 KWNNHHLTFSIQNYTEKLGWYHSMEAVRRAFRVWEQATPLVFQEVPYedirlrrQKEADIMVLFASGFHGDSSPFDGTGG 217
Cdd:cd04278     1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTS-------GQEADIRISFARGNHGDGYPFDGPGG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373 218 FLAHAYFPGpGLGGDTHFDADEPWTFSSTDlHGNNLFLVAVHELGHALGLEHSSNPNAIMAPFYQWKDVdNFKLPEDDLR 297
Cdd:cd04278    74 TLAHAFFPG-GIGGDIHFDDDEQWTLGSDS-GGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIR 150


                  ....*..
gi 1622914373 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 3.49e-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: 242.22  E-value: 3.49e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373 367 PNICDGD-FDTVAMLRGEMFVFKGRWFWRVRHNRVlDNYPMPIGHFWRGLPSDISAAYER-QDGRFVFFKGDRYWLFREA 444
Cdd:cd00094     1 PDACDPLsFDAVTTLRGELYFFKGRYFWRLSPGKP-PGSPFLISSFWPSLPSPVDAAFERpDTGKIYFFKGDKYWVYTGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373 445 NLEPGYPQPLTSYGLGIPYDRIDTAIWWEPTGHTFFFQEDRYWRFNEETQRGDPGYPKSIS-IWQGIPASPKGAFLSNDa 523
Cdd:cd00094    80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIEtDFPGVPDKVDAAFRWLD- 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622914373 524 AYTYFYKGTKYWKFDNERLRMEPGYPKSILRDFMGC 559
Cdd:cd00094   159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 137-304 1.06e-31

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: 120.15  E-value: 1.06e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373  137 RKWNNHHLTFSIqnYTEKLGWYhSMEAVRRAFRVWEQATPLVFQEVPYEdirlrrqkeADIMVLFASGFHGdsspfdgtg 216
Cdd:smart00235   3 KKWPKGTVPYVI--DSSSLSPE-EREAIAKALAEWSDVTCIRFVERTGT---------ADIYISFGSGDSG--------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373  217 GFLAHAYFPGpglgGDTHFDaDEPWTFSSTdlhgnnlflVAVHELGHALGLEHSSNPNA---IMAPFYQWKDVDNFKLPE 293
Cdd:smart00235  62 CTLSHAGRPG----GDQHLS-LGNGCINTG---------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSE 127

                          170
                   ....*....|.
gi 1622914373  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 1622914373 157 WYHSM-EAVRRAFRVWEQATPLVFQEVPyedirlRRQKEADIMVLFasgfhGDSSPFDGTGGFLAHAYFPGPGLGGDT-- 233
Cdd:cd04279    18 RAQSWlQAVKQAAAEWENVGPLKFVYNP------EEDNDADIVIFF-----DRPPPVGGAGGGLARAGFPLISDGNRKlf 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622914373 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 3.71e-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: 71.29  E-value: 3.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373 162 EAVRRAFRVWEQATPLVFQEVPYEDirlrrqkEADIMvlfasgFHGDSSPFDGTGGFlahAYFPGPG----LGGDTHFDA 237
Cdd:cd04277    37 AAARDALEAWEDVADIDFVEVSDNS-------GADIR------FGNSSDPDGNTAGY---AYYPGSGsgtaYGGDIWFNS 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373 238 DEPWTFSSTdlhGNNLFLVAVHELGHALGLEHS-----SNPNAIMAPFYQWKD-------------VDNFKLPE----DD 295
Cdd:cd04277   101 SYDTNSDSP---GSYGYQTIIHEIGHALGLEHPgdyngGDPVPPTYALDSREYtvmsynsgygngaSAGGGYPQtpmlLD 177


                  ....*....
gi 1622914373 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 1622914373 643 TYALVQMQRKGAPRVLLYCKRSLQEWV 669
Cdd:pfam11857  46 IYAIVQFQRKGTPRRLLYCKRSLQDWV 72
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 162-303 2.82e-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: 62.54  E-value: 2.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373 162 EAVRRAFRVWEQATPLVFQEVPYEDIRlrrqkeADIMVLFASGfhgdsspfDGTGGFLAHAYFPG--PGLGGDTHFDADE 239
Cdd:cd00203    25 SLILIAMQIWRDYLNIRFVLVGVEIDK------ADIAILVTRQ--------DFDGGTGGWAYLGRvcDSLRGVGVLQDNQ 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373 240 PWTFsstdlhgnNLFLVAVHELGHALGLEHSSNPNA--------------------IMAPFY-QWKDVDNFKLPEDDLRG 298
Cdd:cd00203    91 SGTK--------EGAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKgSFSDGQRKDFSQCDIDQ 162


                  ....*
gi 1622914373 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 9.02e-11

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: 9.02e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1622914373  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 1.52e-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: 1.52e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1622914373 466 IDTAIWWEPtGHTFFFQEDRYWRFNEETQrgDPGYPKSISIWQGIP 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 1.80e-09

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 53.34  E-value: 1.80e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1622914373 419 ISAAYERQDGRFVFFKGDRYWLFREANLEPGYPQPLTSYgLGIP 462
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKLISDF-PGLP 43
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 53-106 1.36e-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: 1.36e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622914373  53 AENWLRLYGYLPQPSrhmsTMRSAQILASALAEMQRFYGIPVTGVLDEETKEWM 106
Cdd:pfam01471   8 LQRYLNRLGYYPGPV----DGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 466-511 2.18e-08

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: 50.32  E-value: 2.18e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1622914373  466 IDTAIWWEPtGHTFFFQEDRYWRFNEetQRGDPGYPKSIS-IWQGIP 511
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDP--KRVDPGYPKLISsFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 374-417 2.58e-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: 2.58e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1622914373 374 FDTVAMLR-GEMFVFKGRWFWRVRHNRVLDNYPMPIGHFwRGLPS 417
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVEPGYPKLISDF-PGLPC 44
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 162-271 3.27e-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: 3.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373 162 EAVRRAFRVWEQATPLVFQEVpyedirlRRQKEADIMVlfasGFHGDSSPFDGTGGFLAHAYFPGPGlggdTHFDADEPW 241
Cdd:cd04268    18 AAILDAIEAWNKAFAIGFKNA-------NDVDPADIRY----SVIRWIPYNDGTWSYGPSQVDPLTG----EILLARVYL 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 1622914373 242 TFSSTDLHGNNLFLVAVHELGHALGLEHSS 271
Cdd:cd04268    83 YSSFVEYSGARLRNTAEHELGHALGLRHNF 112
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 522-558 2.53e-07

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 47.62  E-value: 2.53e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1622914373  522 DAAY------TYFYKGTKYWKFDNErlRMEPGYPKSILRDFMG 558
Cdd:smart00120   2 DAAFelrdgkTYFFKGDKYWRFDPK--RVDPGYPKLISSFFPG 42
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 374-417 4.60e-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: 4.60e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1622914373  374 FDTVAMLR-GEMFVFKGRWFWRVRHNRVLDNYPMPIGHFWRGLPS 417
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 522-559 8.29e-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: 46.02  E-value: 8.29e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1622914373 522 DAAY------TYFYKGTKYWKFDNErlRMEPGYPKSILRD-FMGC 559
Cdd:pfam00045   2 DAAFedrdgkTYFFKGRKYWRFDPQ--RVEPGYPKLISDFpGLPC 44
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 1622914373 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 1622914373 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 1622914373 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 1.53e-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: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373 162 EAVRRAFRVWEQATPLVFQEVPYEDirlrrqkeADIMVLFASGfHGDSSpFDGTGGFLAHAYFPGPGLGGDTHFDADEpw 241
Cdd:cd04327    23 DKVRAAAREWLPYANLKFKFVTDAD--------ADIRISFTPG-DGYWS-YVGTDALLIGADAPTMNLGWFTDDTPDP-- 90

                          90       100
                  ....*....|....*....|....*...
gi 1622914373 242 TFSSTdlhgnnlflvAVHELGHALGLEH 269
Cdd:cd04327    91 EFSRV----------VLHEFGHALGFIH 108
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 162-279 2.98e-03

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 39.67  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914373 162 EAVRRAFRVWEQATPLvfQEVpyedirlrRQKE-ADIMVLFAS---GFHGDSSP----------FDGTGGFLAHayfpgp 227
Cdd:COG5549   104 AAVLQAIAEWNAYLPL--EVV--------ENPEnADIIIVRSNpplTASPNPETgarsaettyeFYDTGNILSH------ 167

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622914373 228 glggdthfdadepwTFS---STDLHGNNLFLVAVHELGHALGLE-HSSNPNAIMAP 279
Cdd:COG5549   168 --------------RFTillSPNQTGKYLLATARHELGHALGIWgHSPSPTDAMYF 209
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 257-277 4.41e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 38.85  E-value: 4.41e-03
                          10        20
                  ....*....|....*....|.
gi 1622914373 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 1622914373 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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