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Conserved domains on  [gi|1720397594|ref|XP_030104072|]
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matrix metalloproteinase-24 isoform X1 [Mus musculus]

Protein Classification

matrix metalloproteinase( domain architecture ID 12021147)

matrix metalloproteinase is an M10A family metallopeptidase with a C-terminal hemopexin repeat-containing domain, such as stromelysin-1 (matrix metalloproteinase-3), which can degrade fibronectin, laminin, type I, III, IV, and V gelatins, collagens III, IV, X, and IX, as well as cartilage proteoglycans

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 ...
 135-300 1.32e-94

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: 284.51  E-value: 1.32e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594 135 KWRQKHITYSIHNYTPKVGELDTRKAIRQAFDVWQKVTPLTFEEVPYheiksdrKEADIMIFFASGFHGDSSPFDGEGGF 214
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVST-------GEADIMIGFGRGDHGDGYPFDGPGGV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594 215 LAHAYFPGPGIGGDTHFDSDEPWTLGNANHDGNDLFLVAVHELGHALGLEHSNDPSAIMAPFYQYMETHNFKLPQDDLQG 294
Cdd:pfam00413  74 LAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKG 153


                  ....*.
gi 1720397594 295 IQKIYG 300
Cdd:pfam00413 154 IQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 350-506 5.99e-57

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: 188.29  E-value: 5.99e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594 350 PNICDG-NFNTVALFRGEMFVFKDRWFWRLRNNRvQEGYPMQIEQFWKGLPARIDAAYERAD-GRFVFFKGDKYWVFKEV 427
Cdd:cd00094     1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGK-PPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594 428 TVEPGYPHSLGELGSCLPREGIDTALRWEPVGKTYFFKGERYWRYSEERRATDPGYPK-PITVWKGIPQAPQGAFISKEG 506
Cdd:cd00094    80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKlIETDFPGVPDKVDAAFRWLDG 159
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 55-107 2.84e-09

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


:

Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 52.90  E-value: 2.84e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720397594  55 QNWLKSYGYllpYESRASAlHSGKALQSAVSTMQQFYGIPVTGVLDQTTIEWM 107
Cdd:pfam01471   9 QRYLNRLGY---YPGPVDG-YFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 135-300 1.32e-94

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: 284.51  E-value: 1.32e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594 135 KWRQKHITYSIHNYTPKVGELDTRKAIRQAFDVWQKVTPLTFEEVPYheiksdrKEADIMIFFASGFHGDSSPFDGEGGF 214
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVST-------GEADIMIGFGRGDHGDGYPFDGPGGV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594 215 LAHAYFPGPGIGGDTHFDSDEPWTLGNANHDGNDLFLVAVHELGHALGLEHSNDPSAIMAPFYQYMETHNFKLPQDDLQG 294
Cdd:pfam00413  74 LAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKG 153


                  ....*.
gi 1720397594 295 IQKIYG 300
Cdd:pfam00413 154 IQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 135-300 2.17e-88

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: 268.30  E-value: 2.17e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594 135 KWRQKHITYSIHNYTPKVGELDTRKAIRQAFDVWQKVTPLTFEEVPYHEiksdrkEADIMIFFASGFHGDSSPFDGEGGF 214
Cdd:cd04278     1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQ------EADIRISFARGNHGDGYPFDGPGGT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594 215 LAHAYFPGpGIGGDTHFDSDEPWTLGNaNHDGNDLFLVAVHELGHALGLEHSNDPSAIMAPFYQYMEtHNFKLPQDDLQG 294
Cdd:cd04278    75 LAHAFFPG-GIGGDIHFDDDEQWTLGS-DSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV-PKFKLSQDDIRG 151


                  ....*.
gi 1720397594 295 IQKIYG 300
Cdd:cd04278   152 IQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 350-506 5.99e-57

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: 188.29  E-value: 5.99e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594 350 PNICDG-NFNTVALFRGEMFVFKDRWFWRLRNNRvQEGYPMQIEQFWKGLPARIDAAYERAD-GRFVFFKGDKYWVFKEV 427
Cdd:cd00094     1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGK-PPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594 428 TVEPGYPHSLGELGSCLPREGIDTALRWEPVGKTYFFKGERYWRYSEERRATDPGYPK-PITVWKGIPQAPQGAFISKEG 506
Cdd:cd00094    80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKlIETDFPGVPDKVDAAFRWLDG 159
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 134-301 8.99e-36

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: 130.16  E-value: 8.99e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594  134 QKWRQKHITYSIH--NYTPkvgelDTRKAIRQAFDVWQKVTPLTFEEVPYheiksdrkEADIMIFFASGFHGdsspfdge 211
Cdd:smart00235   3 KKWPKGTVPYVIDssSLSP-----EEREAIAKALAEWSDVTCIRFVERTG--------TADIYISFGSGDSG-------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594  212 gGFLAHAYFPGpgigGDTHFDsDEPWTLGNAnhdgndlflVAVHELGHALGLEHSNDPSA---IMAPFYQYMETHNFKLP 288
Cdd:smart00235  62 -CTLSHAGRPG----GDQHLS-LGNGCINTG---------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLS 126

                          170
                   ....*....|...
gi 1720397594  289 QDDLQGIQKIYGP 301
Cdd:smart00235 127 EDDSLGIPYDYGS 139
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 449-494 8.43e-12

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: 59.89  E-value: 8.43e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1720397594 449 IDTALRWEPvGKTYFFKGERYWRYSEERRatDPGYPKPITVWKGIP 494
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQRV--EPGYPKLISDFPGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 449-494 1.37e-10

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 56.48  E-value: 1.37e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1720397594  449 IDTALRWePVGKTYFFKGERYWRYSEERRatDPGYPKPIT-VWKGIP 494
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDPKRV--DPGYPKLISsFFPGLP 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 55-107 2.84e-09

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 52.90  E-value: 2.84e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720397594  55 QNWLKSYGYllpYESRASAlHSGKALQSAVSTMQQFYGIPVTGVLDQTTIEWM 107
Cdd:pfam01471   9 QRYLNRLGY---YPGPVDG-YFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 158-299 2.01e-05

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 45.83  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594 158 RKAIRQAFDVWQKVtpLTFEEVpyheikSDRKEADIMIFFAS---GFHGDSSP----------FDGEGGFLAHAYfpgpg 224
Cdd:COG5549   103 VAAVLQAIAEWNAY--LPLEVV------ENPENADIIIVRSNpplTASPNPETgarsaettyeFYDTGNILSHRF----- 169

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720397594 225 iggdthfdsdepwTLG-NANHDGNDLFLVAVHELGHALGLE-HSNDPSAIMapfyqYME-THNFKLPQD-DLQGIQKIY 299
Cdd:COG5549   170 -------------TILlSPNQTGKYLLATARHELGHALGIWgHSPSPTDAM-----YFSqVRNPPPISPrDINTLKRIY 230
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
245-273 1.51e-04

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 42.61  E-value: 1.51e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1720397594 245 DGNDLFL-----VAVHELGHALGLEHSNDPSAIM 273
Cdd:NF033823  113 PDEDLFLerlakEAVHELGHLLGLGHCPNPRCVM 146
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 253-273 1.46e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 39.62  E-value: 1.46e-03
                          10        20
                  ....*....|....*....|.
gi 1720397594 253 AVHELGHALGLEHSNDPSAIM 273
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 ...
 135-300 1.32e-94

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: 284.51  E-value: 1.32e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594 135 KWRQKHITYSIHNYTPKVGELDTRKAIRQAFDVWQKVTPLTFEEVPYheiksdrKEADIMIFFASGFHGDSSPFDGEGGF 214
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVST-------GEADIMIGFGRGDHGDGYPFDGPGGV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594 215 LAHAYFPGPGIGGDTHFDSDEPWTLGNANHDGNDLFLVAVHELGHALGLEHSNDPSAIMAPFYQYMETHNFKLPQDDLQG 294
Cdd:pfam00413  74 LAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKG 153


                  ....*.
gi 1720397594 295 IQKIYG 300
Cdd:pfam00413 154 IQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 135-300 2.17e-88

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: 268.30  E-value: 2.17e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594 135 KWRQKHITYSIHNYTPKVGELDTRKAIRQAFDVWQKVTPLTFEEVPYHEiksdrkEADIMIFFASGFHGDSSPFDGEGGF 214
Cdd:cd04278     1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQ------EADIRISFARGNHGDGYPFDGPGGT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594 215 LAHAYFPGpGIGGDTHFDSDEPWTLGNaNHDGNDLFLVAVHELGHALGLEHSNDPSAIMAPFYQYMEtHNFKLPQDDLQG 294
Cdd:cd04278    75 LAHAFFPG-GIGGDIHFDDDEQWTLGS-DSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV-PKFKLSQDDIRG 151


                  ....*.
gi 1720397594 295 IQKIYG 300
Cdd:cd04278   152 IQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 350-506 5.99e-57

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: 188.29  E-value: 5.99e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594 350 PNICDG-NFNTVALFRGEMFVFKDRWFWRLRNNRvQEGYPMQIEQFWKGLPARIDAAYERAD-GRFVFFKGDKYWVFKEV 427
Cdd:cd00094     1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGK-PPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594 428 TVEPGYPHSLGELGSCLPREGIDTALRWEPVGKTYFFKGERYWRYSEERRATDPGYPK-PITVWKGIPQAPQGAFISKEG 506
Cdd:cd00094    80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKlIETDFPGVPDKVDAAFRWLDG 159
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 134-301 8.99e-36

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: 130.16  E-value: 8.99e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594  134 QKWRQKHITYSIH--NYTPkvgelDTRKAIRQAFDVWQKVTPLTFEEVPYheiksdrkEADIMIFFASGFHGdsspfdge 211
Cdd:smart00235   3 KKWPKGTVPYVIDssSLSP-----EEREAIAKALAEWSDVTCIRFVERTG--------TADIYISFGSGDSG-------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594  212 gGFLAHAYFPGpgigGDTHFDsDEPWTLGNAnhdgndlflVAVHELGHALGLEHSNDPSA---IMAPFYQYMETHNFKLP 288
Cdd:smart00235  62 -CTLSHAGRPG----GDQHLS-LGNGCINTG---------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLS 126

                          170
                   ....*....|...
gi 1720397594  289 QDDLQGIQKIYGP 301
Cdd:smart00235 127 EDDSLGIPYDYGS 139
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 141-300 8.75e-19

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: 84.39  E-value: 8.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594 141 ITYSIHNYTPKV------GELDT---------RKAIRQAFDVWQKVTPLTFEEVPYHEiksdrkEADIMIFFASGFHGDS 205
Cdd:cd04277     4 LTYSFSNTGGPYsygygrEEDTTntaalsaaqQAAARDALEAWEDVADIDFVEVSDNS------GADIRFGNSSDPDGNT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594 206 spfdgeggfLAHAYFPGPGI----GGDTHFDSDEpwtLGNANHDGNDLFLVAVHELGHALGLEHSNDPSA---------- 271
Cdd:cd04277    78 ---------AGYAYYPGSGSgtayGGDIWFNSSY---DTNSDSPGSYGYQTIIHEIGHALGLEHPGDYNGgdpvpptyal 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1720397594 272 ------IMAPFYQY--METHNFKLPQD----DLQGIQKIYG 300
Cdd:cd04277   146 dsreytVMSYNSGYgnGASAGGGYPQTpmllDIAALQYLYG 186
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 159-300 2.73e-18

Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239806 [Multi-domain]  Cd Length: 156  Bit Score: 81.73  E-value: 2.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594 159 KAIRQAFDVWQKVTPLTFEEVPYHEiksdrKEADIMIFFasgfhGDSSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWT 238
Cdd:cd04279    24 QAVKQAAAEWENVGPLKFVYNPEED-----NDADIVIFF-----DRPPPVGGAGGGLARAGFPLISDGNRKLFNRTDINL 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720397594 239 LGNANHDGNDLFLVAVHELGHALGLEHSND-PSAIMAPFYQYMETHNFKLPQDDLQGIQKIYG 300
Cdd:cd04279    94 GPGQPRGAENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 141-299 1.25e-14

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: 71.78  E-value: 1.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594 141 ITYSIHNYTPKVGELDT----RKAIRQAFDVWQKVTPLTFEEVPYHEIKsdrkeADIMIFFASGfhgdsspfDGEGGFLA 216
Cdd:cd00203     3 IPYVVVADDRDVEEENLsaqiQSLILIAMQIWRDYLNIRFVLVGVEIDK-----ADIAILVTRQ--------DFDGGTGG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594 217 HAYFPG--PGIGGDTHFDSDEPWTlgnanhdgNDLFLVAVHELGHALGLEHSNDPSA--------------------IMA 274
Cdd:cd00203    70 WAYLGRvcDSLRGVGVLQDNQSGT--------KEGAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMS 141

                         170       180
                  ....*....|....*....|....*.
gi 1720397594 275 PFY-QYMETHNFKLPQDDLQGIQKIY 299
Cdd:cd00203   142 YTKgSFSDGQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 138-299 3.52e-12

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: 64.44  E-value: 3.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594 138 QKHITYSIHNYTPKvgelDTRKAIRQAFDVWQKVTPLTFEEVPyheiksDRKEADIMIFFASGFHGDsspfDGEGGFLAH 217
Cdd:cd04268     1 KKPITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNAN------DVDPADIRYSVIRWIPYN----DGTWSYGPS 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594 218 AYFPGPG--IGGDTHFDSDEPWTLGNANHDgndlflVAVHELGHALGLEHSNDPSAIMAPFYQYMETH-----------N 284
Cdd:cd04268    67 QVDPLTGeiLLARVYLYSSFVEYSGARLRN------TAEHELGHALGLRHNFAASDRDDNVDLLAEKGdtssvmdyapsN 140

                         170       180
                  ....*....|....*....|....*
gi 1720397594 285 FKLPQ----------DDLQGIQKIY 299
Cdd:cd04268   141 FSIQLgdgqkytigpYDIAAIKKLY 165
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 449-494 8.43e-12

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: 59.89  E-value: 8.43e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1720397594 449 IDTALRWEPvGKTYFFKGERYWRYSEERRatDPGYPKPITVWKGIP 494
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQRV--EPGYPKLISDFPGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 449-494 1.37e-10

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 56.48  E-value: 1.37e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1720397594  449 IDTALRWePVGKTYFFKGERYWRYSEERRatDPGYPKPIT-VWKGIP 494
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDPKRV--DPGYPKLISsFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 402-440 3.02e-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: 55.27  E-value: 3.02e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1720397594 402 IDAAYERADGRFVFFKGDKYWVFKEVTVEPGYPHSLGEL 440
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKLISDF 39
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 402-446 1.43e-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: 53.40  E-value: 1.43e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1720397594  402 IDAAYERADGRFVFFKGDKYWVFKEVTVEPGYPHSLGELGSCLPR 446
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 55-107 2.84e-09

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 52.90  E-value: 2.84e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720397594  55 QNWLKSYGYllpYESRASAlHSGKALQSAVSTMQQFYGIPVTGVLDQTTIEWM 107
Cdd:pfam01471   9 QRYLNRLGY---YPGPVDG-YFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 364-399 1.68e-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: 1.68e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1720397594  364 RGEMFVFKDRWFWRLRNNRVQEGYPMQIEQFWKGLP 399
Cdd:smart00120   9 DGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 362-399 4.27e-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: 46.41  E-value: 4.27e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1720397594 362 LFRGEMFVFKDRWFWRLRNNRVQEGYPMQIEQFWkGLP 399
Cdd:pfam00045   7 DRDGKTYFFKGRKYWRFDPQRVEPGYPKLISDFP-GLP 43
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 158-299 2.01e-05

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 45.83  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594 158 RKAIRQAFDVWQKVtpLTFEEVpyheikSDRKEADIMIFFAS---GFHGDSSP----------FDGEGGFLAHAYfpgpg 224
Cdd:COG5549   103 VAAVLQAIAEWNAY--LPLEVV------ENPENADIIIVRSNpplTASPNPETgarsaettyeFYDTGNILSHRF----- 169

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720397594 225 iggdthfdsdepwTLG-NANHDGNDLFLVAVHELGHALGLE-HSNDPSAIMapfyqYME-THNFKLPQD-DLQGIQKIY 299
Cdd:COG5549   170 -------------TILlSPNQTGKYLLATARHELGHALGIWgHSPSPTDAM-----YFSqVRNPPPISPrDINTLKRIY 230
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
245-273 1.51e-04

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 42.61  E-value: 1.51e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1720397594 245 DGNDLFL-----VAVHELGHALGLEHSNDPSAIM 273
Cdd:NF033823  113 PDEDLFLerlakEAVHELGHLLGLGHCPNPRCVM 146
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 153-265 1.92e-04

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: 42.75  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397594 153 GELDTRKAIRQAFDVWQKVTPLTFEEVpyheiksDRKEADIMIFFASGfHGDSSpFDGEGGFLAHAYFPGPGIGGDTHFD 232
Cdd:cd04327    17 PDAFLKDKVRAAAREWLPYANLKFKFV-------TDADADIRISFTPG-DGYWS-YVGTDALLIGADAPTMNLGWFTDDT 87

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1720397594 233 SDepwtlgnanhdgNDLFLVAVHELGHALGLEH 265
Cdd:cd04327    88 PD------------PEFSRVVLHEFGHALGFIH 108
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
248-275 2.67e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 41.87  E-value: 2.67e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1720397594 248 DLFL-----VAVHELGHALGLEHSNDPSAIMAP 275
Cdd:COG1913   117 ELFLervlkEAVHELGHLFGLGHCPNPRCVMHF 149
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 253-273 1.46e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 39.62  E-value: 1.46e-03
                          10        20
                  ....*....|....*....|.
gi 1720397594 253 AVHELGHALGLEHSNDPSAIM 273
Cdd:PRK13267  129 VTHELGHTLGLEHCDNPRCVM 149
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 245-275 2.00e-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: 39.20  E-value: 2.00e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1720397594 245 DGNDLFL-----VAVHELGHALGLEHSNDPSAIMAP 275
Cdd:cd11375   114 PDEGLFLerllkEAVHELGHLFGLDHCPYYACVMNF 149
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
 209-265 4.92e-03

Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma protein A (PAPP-A or pappalysin-1) cleaves insulin-like growth factor-binding proteins 4 and 5, thereby promoting cell growth by releasing bound growth factor. This model includes pappalysins and related metalloprotease domains from all three kingdoms of life. The three-dimensional structure of an archaeal representative, ulilysin, has been solved.


Pssm-ID: 239802 [Multi-domain]  Cd Length: 225  Bit Score: 38.47  E-value: 4.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720397594 209 DGEGGFLAHAYFPGPGIGGDTHFD--SDEPWTLGNANHDGNDLFLVAVHELGHALGLEH 265
Cdd:cd04275    95 FLGGGLLGYATFPDSLVSLAFITDgvVINPSSLPGGSAAPYNLGDTATHEVGHWLGLYH 153
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 244-276 9.56e-03

Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 37.59  E-value: 9.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1720397594 244 HDGNDLFLVAV---HELGHALGLEHSN------DPSAIMAPF 276
Cdd:cd04269   123 DHSRNLLLFAVtmaHELGHNLGMEHDDggctcgRSTCIMAPS 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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