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Conserved domains on  [gi|115392138|ref|NP_032631|]
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macrophage metalloelastase isoform 1 preproprotein [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 ...
 112-267 1.97e-95

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: 284.89  E-value: 1.97e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115392138  112 RWMKRYLTYRIYNYTPDMKREDVDYIFQKAFQVWSDVTPLRFRKLHKDEADIMILFAFGAHGDFNYFDGKGGTLAHAFYP 191
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115392138  192 GPGIQGDAHFDEAETWTKS---FQGTNLFLVAVHELGHSLGLQHSNNPKSIMYPTYRYLNPSTFRLSADDIRNIQSLYG 267
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGsdpPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 289-473 1.32e-59

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: 194.07  E-value: 1.32e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115392138 289 SLSFDAVTTVGEKIFFFKDWFFWWKLPGSPATNITSISSIWPSIPSGIQAAYEIESRNQLFLFKDEKYWLINNLVPEPHY 368
Cdd:cd00094    6 PLSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGKNLEPGY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115392138 369 PRSIYSLGFSASVKKVDAAVFDPLRQKVYFFVDKHYWRYDVRQELMDPAYPKLISTHFPGIKPKIDAVLYFKR-HYYIFQ 447
Cdd:cd00094   86 PKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDgYYYFFK 165

                        170       180
                 ....*....|....*....|....*....
gi 115392138 448 GAYQLEYDPLFR--RVTKTLKSTS-WFGC 473
Cdd:cd00094  166 GDQYWRFDPRSKevRVGYPLKISSdWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 37-91 1.62e-07

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: 47.90  E-value: 1.62e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 115392138   37 AEWYLSRFYDYgkdriPMTKTKTNRNFLKEKLQEMQQFFGLEATGQLDNSTLAIM 91
Cdd:pfam01471   8 LQRYLNRLGYY-----PGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 112-267 1.97e-95

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: 284.89  E-value: 1.97e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115392138  112 RWMKRYLTYRIYNYTPDMKREDVDYIFQKAFQVWSDVTPLRFRKLHKDEADIMILFAFGAHGDFNYFDGKGGTLAHAFYP 191
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115392138  192 GPGIQGDAHFDEAETWTKS---FQGTNLFLVAVHELGHSLGLQHSNNPKSIMYPTYRYLNPSTFRLSADDIRNIQSLYG 267
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGsdpPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 112-267 1.74e-79

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: 244.04  E-value: 1.74e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115392138 112 RWMKRYLTYRIYNYTPDMKREDVDYIFQKAFQVWSDVTPLRFRKLH-KDEADIMILFAFGAHGDFNYFDGKGGTLAHAFY 190
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTsGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115392138 191 PGpGIQGDAHFDEAETWTKS--FQGTNLFLVAVHELGHSLGLQHSNNPKSIMYPTYRYLNPStFRLSADDIRNIQSLYG 267
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTLGsdSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK-FKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 289-473 1.32e-59

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: 194.07  E-value: 1.32e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115392138 289 SLSFDAVTTVGEKIFFFKDWFFWWKLPGSPATNITSISSIWPSIPSGIQAAYEIESRNQLFLFKDEKYWLINNLVPEPHY 368
Cdd:cd00094    6 PLSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGKNLEPGY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115392138 369 PRSIYSLGFSASVKKVDAAVFDPLRQKVYFFVDKHYWRYDVRQELMDPAYPKLISTHFPGIKPKIDAVLYFKR-HYYIFQ 447
Cdd:cd00094   86 PKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDgYYYFFK 165

                        170       180
                 ....*....|....*....|....*....
gi 115392138 448 GAYQLEYDPLFR--RVTKTLKSTS-WFGC 473
Cdd:cd00094  166 GDQYWRFDPRSKevRVGYPLKISSdWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 112-268 9.22e-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: 118.61  E-value: 9.22e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115392138   112 RWMKRYLTYRIYnyTPDMKReDVDYIFQKAFQVWSDVTPLRFRKLHkDEADIMILFAFGAHGDFnyfdgkggtLAHAFYP 191
Cdd:smart00235   4 KWPKGTVPYVID--SSSLSP-EEREAIAKALAEWSDVTCIRFVERT-GTADIYISFGSGDSGCT---------LSHAGRP 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115392138   192 GpgiqGDAHFDEaETWTKSFQgtnlflVAVHELGHSLGLQHSNNPKS---IMYPTYRYLNPSTFRLSADDIRNIQSLYGA 268
Cdd:smart00235  71 G----GDQHLSL-GNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYDYGS 139
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 384-429 3.57e-10

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 54.94  E-value: 3.57e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 115392138   384 VDAAVFDPlRQKVYFFVDKHYWRYDVRQelMDPAYPKLISTHFPGI 429
Cdd:smart00120   1 IDAAFELR-DGKTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGL 43
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 384-429 1.92e-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: 1.92e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 115392138  384 VDAAVFDPlRQKVYFFVDKHYWRYDVRQelMDPAYPKLIStHFPGI 429
Cdd:pfam00045   1 IDAAFEDR-DGKTYFFKGRKYWRFDPQR--VEPGYPKLIS-DFPGL 42
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 37-91 1.62e-07

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: 47.90  E-value: 1.62e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 115392138   37 AEWYLSRFYDYgkdriPMTKTKTNRNFLKEKLQEMQQFFGLEATGQLDNSTLAIM 91
Cdd:pfam01471   8 LQRYLNRLGYY-----PGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 138-270 6.03e-07

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 50.45  E-value: 6.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115392138 138 FQKAFQVWSDVTPLRFRKlHKDEADIMILFA---FGAHGDFNyfdgKGGTLAHAFYPgPGIQGDAHFDEAETWTKSFQgT 214
Cdd:COG5549  106 VLQAIAEWNAYLPLEVVE-NPENADIIIVRSnppLTASPNPE----TGARSAETTYE-FYDTGNILSHRFTILLSPNQ-T 178

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 115392138 215 NLFLVAV--HELGHSLGLQ-HSNNPKSIMYPTYRYLNPstfRLSADDIRNIQSLYGAPV 270
Cdd:COG5549  179 GKYLLATarHELGHALGIWgHSPSPTDAMYFSQVRNPP---PISPRDINTLKRIYQQPT 234
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
220-241 7.55e-05

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 43.38  E-value: 7.55e-05
                         10        20
                 ....*....|....*....|..
gi 115392138 220 AVHELGHSLGLQHSNNPKSIMY 241
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 220-241 2.29e-04

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 41.93  E-value: 2.29e-04
                         10        20
                 ....*....|....*....|..
gi 115392138 220 AVHELGHSLGLQHSNNPKSIMY 241
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVMN 150
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 112-267 1.97e-95

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: 284.89  E-value: 1.97e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115392138  112 RWMKRYLTYRIYNYTPDMKREDVDYIFQKAFQVWSDVTPLRFRKLHKDEADIMILFAFGAHGDFNYFDGKGGTLAHAFYP 191
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115392138  192 GPGIQGDAHFDEAETWTKS---FQGTNLFLVAVHELGHSLGLQHSNNPKSIMYPTYRYLNPSTFRLSADDIRNIQSLYG 267
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGsdpPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 112-267 1.74e-79

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: 244.04  E-value: 1.74e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115392138 112 RWMKRYLTYRIYNYTPDMKREDVDYIFQKAFQVWSDVTPLRFRKLH-KDEADIMILFAFGAHGDFNYFDGKGGTLAHAFY 190
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTsGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115392138 191 PGpGIQGDAHFDEAETWTKS--FQGTNLFLVAVHELGHSLGLQHSNNPKSIMYPTYRYLNPStFRLSADDIRNIQSLYG 267
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTLGsdSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK-FKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 289-473 1.32e-59

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: 194.07  E-value: 1.32e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115392138 289 SLSFDAVTTVGEKIFFFKDWFFWWKLPGSPATNITSISSIWPSIPSGIQAAYEIESRNQLFLFKDEKYWLINNLVPEPHY 368
Cdd:cd00094    6 PLSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGKNLEPGY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115392138 369 PRSIYSLGFSASVKKVDAAVFDPLRQKVYFFVDKHYWRYDVRQELMDPAYPKLISTHFPGIKPKIDAVLYFKR-HYYIFQ 447
Cdd:cd00094   86 PKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDgYYYFFK 165

                        170       180
                 ....*....|....*....|....*....
gi 115392138 448 GAYQLEYDPLFR--RVTKTLKSTS-WFGC 473
Cdd:cd00094  166 GDQYWRFDPRSKevRVGYPLKISSdWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 112-268 9.22e-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: 118.61  E-value: 9.22e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115392138   112 RWMKRYLTYRIYnyTPDMKReDVDYIFQKAFQVWSDVTPLRFRKLHkDEADIMILFAFGAHGDFnyfdgkggtLAHAFYP 191
Cdd:smart00235   4 KWPKGTVPYVID--SSSLSP-EEREAIAKALAEWSDVTCIRFVERT-GTADIYISFGSGDSGCT---------LSHAGRP 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115392138   192 GpgiqGDAHFDEaETWTKSFQgtnlflVAVHELGHSLGLQHSNNPKS---IMYPTYRYLNPSTFRLSADDIRNIQSLYGA 268
Cdd:smart00235  71 G----GDQHLSL-GNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYDYGS 139
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 139-267 1.10e-19

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: 85.59  E-value: 1.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115392138 139 QKAFQVWSDVTPLRFRK--LHKDEADIMILFAFGAHGDfnyfdGKGGTLAHAFYPGPGIQGDA---HFDEAETWTKSFQG 213
Cdd:cd04279   27 KQAAAEWENVGPLKFVYnpEEDNDADIVIFFDRPPPVG-----GAGGGLARAGFPLISDGNRKlfnRTDINLGPGQPRGA 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 115392138 214 TNLFLVAVHELGHSLGLQH-SNNPKSIMYPTYRYLNPSTFRLSADDIRNIQSLYG 267
Cdd:cd04279  102 ENLQAIALHELGHALGLWHhSDRPEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 140-267 3.10e-16

Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 76.69  E-value: 3.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115392138 140 KAFQVWSDVTPLRFRKL-HKDEADIMIlfafgahgdFNYFDGKGGTLAHAFYPGPGI----QGDAHFDEAETWTKSFQGT 214
Cdd:cd04277   41 DALEAWEDVADIDFVEVsDNSGADIRF---------GNSSDPDGNTAGYAYYPGSGSgtayGGDIWFNSSYDTNSDSPGS 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115392138 215 NLFLVAVHELGHSLGLQHS----------------NNPKSIMypTYR----------YLNPSTFRLsaDDIRNIQSLYG 267
Cdd:cd04277  112 YGYQTIIHEIGHALGLEHPgdynggdpvpptyaldSREYTVM--SYNsgygngasagGGYPQTPML--LDIAALQYLYG 186
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 116-266 5.25e-12

Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 64.08  E-value: 5.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115392138 116 RYLTYRIYNYTPDMKRED----VDYIFQKAFQVWSDVTPLRF--RKLHKDEADIMILFAfgahgdfnYFDGKGGTLAHAF 189
Cdd:cd00203    1 KVIPYVVVADDRDVEEENlsaqIQSLILIAMQIWRDYLNIRFvlVGVEIDKADIAILVT--------RQDFDGGTGGWAY 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115392138 190 YPG--PGIQGDAHFDEAETWTKSFqgtnlFLVAVHELGHSLGLQHSNNPK--------------------SIMYPTY-RY 246
Cdd:cd00203   73 LGRvcDSLRGVGVLQDNQSGTKEG-----AQTIAHELGHALGFYHDHDRKdrddyptiddtlnaedddyySVMSYTKgSF 147

                        170       180
                 ....*....|....*....|
gi 115392138 247 LNPSTFRLSADDIRNIQSLY 266
Cdd:cd00203  148 SDGQRKDFSQCDIDQINKLY 167
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 384-429 3.57e-10

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 54.94  E-value: 3.57e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 115392138   384 VDAAVFDPlRQKVYFFVDKHYWRYDVRQelMDPAYPKLISTHFPGI 429
Cdd:smart00120   1 IDAAFELR-DGKTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGL 43
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 115-266 5.13e-09

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: 55.20  E-value: 5.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115392138 115 KRYLTYRIYNYTPDmkreDVDYIFQKAFQVWSDVTPLRFRK-LHKDEADIMIlfafgahgdFNYFDGKGGTLAHAFYPGp 193
Cdd:cd04268    1 KKPITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNaNDVDPADIRY---------SVIRWIPYNDGTWSYGPS- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115392138 194 giqgDAHFDEAETWTKSFQGTNLFL---------VAVHELGHSLGLQHSNNPK----------------SIMYPTYRYLN 248
Cdd:cd04268   67 ----QVDPLTGEILLARVYLYSSFVeysgarlrnTAEHELGHALGLRHNFAASdrddnvdllaekgdtsSVMDYAPSNFS 142

                        170       180
                 ....*....|....*....|...
gi 115392138 249 PSTF-----RLSADDIRNIQSLY 266
Cdd:cd04268  143 IQLGdgqkyTIGPYDIAAIKKLY 165
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 384-429 1.92e-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: 1.92e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 115392138  384 VDAAVFDPlRQKVYFFVDKHYWRYDVRQelMDPAYPKLIStHFPGI 429
Cdd:pfam00045   1 IDAAFEDR-DGKTYFFKGRKYWRFDPQR--VEPGYPKLIS-DFPGL 42
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 37-91 1.62e-07

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: 47.90  E-value: 1.62e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 115392138   37 AEWYLSRFYDYgkdriPMTKTKTNRNFLKEKLQEMQQFFGLEATGQLDNSTLAIM 91
Cdd:pfam01471   8 LQRYLNRLGYY-----PGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 138-270 6.03e-07

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 50.45  E-value: 6.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115392138 138 FQKAFQVWSDVTPLRFRKlHKDEADIMILFA---FGAHGDFNyfdgKGGTLAHAFYPgPGIQGDAHFDEAETWTKSFQgT 214
Cdd:COG5549  106 VLQAIAEWNAYLPLEVVE-NPENADIIIVRSnppLTASPNPE----TGARSAETTYE-FYDTGNILSHRFTILLSPNQ-T 178

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 115392138 215 NLFLVAV--HELGHSLGLQ-HSNNPKSIMYPTYRYLNPstfRLSADDIRNIQSLYGAPV 270
Cdd:COG5549  179 GKYLLATarHELGHALGIWgHSPSPTDAMYFSQVRNPP---PISPRDINTLKRIYQQPT 234
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 336-375 1.42e-05

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 42.17  E-value: 1.42e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 115392138  336 IQAAYEIEsRNQLFLFKDEKYWLINNLVPEPHYPRSIYSL 375
Cdd:pfam00045   1 IDAAFEDR-DGKTYFFKGRKYWRFDPQRVEPGYPKLISDF 39
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
219-243 4.49e-05

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 43.79  E-value: 4.49e-05
                         10        20
                 ....*....|....*....|....*
gi 115392138 219 VAVHELGHSLGLQHSNNPKSIMYPT 243
Cdd:COG1913  126 EAVHELGHLFGLGHCPNPRCVMHFS 150
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
220-241 7.55e-05

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 43.38  E-value: 7.55e-05
                         10        20
                 ....*....|....*....|..
gi 115392138 220 AVHELGHSLGLQHSNNPKSIMY 241
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 220-241 2.29e-04

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 41.93  E-value: 2.29e-04
                         10        20
                 ....*....|....*....|..
gi 115392138 220 AVHELGHSLGLQHSNNPKSIMY 241
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVMN 150
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 336-375 3.21e-04

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: 38.38  E-value: 3.21e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 115392138   336 IQAAYEIeSRNQLFLFKDEKYWLINNLVPEPHYPRSIYSL 375
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDPKRVDPGYPKLISSF 39
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 219-243 1.37e-03

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


Pssm-ID: 213029  Cd Length: 173  Bit Score: 39.59  E-value: 1.37e-03
                         10        20
                 ....*....|....*....|....*
gi 115392138 219 VAVHELGHSLGLQHSNNPKSIMYPT 243
Cdd:cd11375  126 EAVHELGHLFGLDHCPYYACVMNFS 150
 
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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