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Conserved domains on  [gi|291327537|ref|NP_446415|]
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macrophage metalloelastase preproprotein [Rattus norvegicus]

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 ...
 116-271 4.05e-96

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: 286.82  E-value: 4.05e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327537  116 RWMKRYLTYRIYNYTPDMKRADVDYIFQKAFQVWSDVTPLRFRKIHKGEADITILFAFGDHGDFYDFDGKGGTLAHAFYP 195
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291327537  196 GPGIQGDAHFDEAETWTKS---FQGTNLFLVAVHELGHSLGLPHSNNPKSIMYPTYRYLHPNTFRLSADDIHSIQSLYG 271
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGsdpPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 293-477 1.18e-60

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: 196.76  E-value: 1.18e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327537 293 SLSFDAVTTVGDKIFFFKDWFFWWRLPGSPATNITSISSMWPTIPSGIQAAYEIGGRNQLFLFKDEKYWLINNLVPEPHY 372
Cdd:cd00094    6 PLSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGKNLEPGY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327537 373 PRSIHSLGFPASVKKIDAAVFDPLRQKVYFFVDKQYWRYDVRQELMDAAYPKLISTHFPGIRPKIDAVLYFKR-HYYIFQ 451
Cdd:cd00094   86 PKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDgYYYFFK 165

                        170       180
                 ....*....|....*....|....*....
gi 291327537 452 GAYQLEYDP--LLHRVTKTLSSTS-WFGC 477
Cdd:cd00094  166 GDQYWRFDPrsKEVRVGYPLKISSdWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 41-95 5.80e-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: 46.35  E-value: 5.80e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 291327537   41 AEWYLSRFFDYQGdripmTKTKTNRNLLEEKLQEMQQFFGLEVTGQLDTSTLKIM 95
Cdd:pfam01471   8 LQRYLNRLGYYPG-----PVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 116-271 4.05e-96

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: 286.82  E-value: 4.05e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327537  116 RWMKRYLTYRIYNYTPDMKRADVDYIFQKAFQVWSDVTPLRFRKIHKGEADITILFAFGDHGDFYDFDGKGGTLAHAFYP 195
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291327537  196 GPGIQGDAHFDEAETWTKS---FQGTNLFLVAVHELGHSLGLPHSNNPKSIMYPTYRYLHPNTFRLSADDIHSIQSLYG 271
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGsdpPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 116-271 1.05e-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: 242.11  E-value: 1.05e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327537 116 RWMKRYLTYRIYNYTPDMKRADVDYIFQKAFQVWSDVTPLRFRKIH-KGEADITILFAFGDHGDFYDFDGKGGTLAHAFY 194
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTsGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291327537 195 PGpGIQGDAHFDEAETWTKS--FQGTNLFLVAVHELGHSLGLPHSNNPKSIMYPTYRYLHPNtFRLSADDIHSIQSLYG 271
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTLGsdSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK-FKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 293-477 1.18e-60

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: 196.76  E-value: 1.18e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327537 293 SLSFDAVTTVGDKIFFFKDWFFWWRLPGSPATNITSISSMWPTIPSGIQAAYEIGGRNQLFLFKDEKYWLINNLVPEPHY 372
Cdd:cd00094    6 PLSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGKNLEPGY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327537 373 PRSIHSLGFPASVKKIDAAVFDPLRQKVYFFVDKQYWRYDVRQELMDAAYPKLISTHFPGIRPKIDAVLYFKR-HYYIFQ 451
Cdd:cd00094   86 PKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDgYYYFFK 165

                        170       180
                 ....*....|....*....|....*....
gi 291327537 452 GAYQLEYDP--LLHRVTKTLSSTS-WFGC 477
Cdd:cd00094  166 GDQYWRFDPrsKEVRVGYPLKISSdWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 116-272 2.42e-30

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: 114.76  E-value: 2.42e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327537   116 RWMKRYLTYRIYnyTPDMKRaDVDYIFQKAFQVWSDVTPLRFRKIHkGEADITILFAFGDHGDFYdfdgkggtlAHAFYP 195
Cdd:smart00235   4 KWPKGTVPYVID--SSSLSP-EEREAIAKALAEWSDVTCIRFVERT-GTADIYISFGSGDSGCTL---------SHAGRP 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327537   196 GpgiqGDAHFDEaETWTKSFQgtnlflVAVHELGHSLGLPHSNNPKS---IMYPTYRYLHPNTFRLSADDIHSIQSLYGA 272
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. ...
 388-433 7.13e-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: 54.17  E-value: 7.13e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 291327537   388 IDAAVFDPlRQKVYFFVDKQYWRYDVRQelMDAAYPKLISTHFPGI 433
Cdd:smart00120   1 IDAAFELR-DGKTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGL 43
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 388-433 2.70e-08

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 49.87  E-value: 2.70e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 291327537  388 IDAAVFDPlRQKVYFFVDKQYWRYDVRQelMDAAYPKLIStHFPGI 433
Cdd:pfam00045   1 IDAAFEDR-DGKTYFFKGRKYWRFDPQR--VEPGYPKLIS-DFPGL 42
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 142-274 1.75e-07

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 51.99  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327537 142 FQKAFQVWSDVtpLRFRKIHKGE-ADITILFA-----FGDHGDF--------YDFDGKGGTLAHAF--YPGPGiQGDahf 205
Cdd:COG5549  106 VLQAIAEWNAY--LPLEVVENPEnADIIIVRSnppltASPNPETgarsaettYEFYDTGNILSHRFtiLLSPN-QTG--- 179

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291327537 206 deaetwtKSFQGTnlflvAVHELGHSLGLP-HSNNPKSIMYP-TYRYLHPntfrLSADDIHSIQSLYGAPV 274
Cdd:COG5549  180 -------KYLLAT-----ARHELGHALGIWgHSPSPTDAMYFsQVRNPPP----ISPRDINTLKRIYQQPT 234
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 41-95 5.80e-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: 46.35  E-value: 5.80e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 291327537   41 AEWYLSRFFDYQGdripmTKTKTNRNLLEEKLQEMQQFFGLEVTGQLDTSTLKIM 95
Cdd:pfam01471   8 LQRYLNRLGYYPG-----PVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
224-245 3.20e-05

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 44.15  E-value: 3.20e-05
                         10        20
                 ....*....|....*....|..
gi 291327537 224 AVHELGHSLGLPHSNNPKSIMY 245
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 224-245 1.34e-04

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 42.70  E-value: 1.34e-04
                         10        20
                 ....*....|....*....|..
gi 291327537 224 AVHELGHSLGLPHSNNPKSIMY 245
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 ...
 116-271 4.05e-96

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: 286.82  E-value: 4.05e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327537  116 RWMKRYLTYRIYNYTPDMKRADVDYIFQKAFQVWSDVTPLRFRKIHKGEADITILFAFGDHGDFYDFDGKGGTLAHAFYP 195
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291327537  196 GPGIQGDAHFDEAETWTKS---FQGTNLFLVAVHELGHSLGLPHSNNPKSIMYPTYRYLHPNTFRLSADDIHSIQSLYG 271
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGsdpPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 116-271 1.05e-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: 242.11  E-value: 1.05e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327537 116 RWMKRYLTYRIYNYTPDMKRADVDYIFQKAFQVWSDVTPLRFRKIH-KGEADITILFAFGDHGDFYDFDGKGGTLAHAFY 194
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTsGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291327537 195 PGpGIQGDAHFDEAETWTKS--FQGTNLFLVAVHELGHSLGLPHSNNPKSIMYPTYRYLHPNtFRLSADDIHSIQSLYG 271
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTLGsdSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK-FKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 293-477 1.18e-60

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: 196.76  E-value: 1.18e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327537 293 SLSFDAVTTVGDKIFFFKDWFFWWRLPGSPATNITSISSMWPTIPSGIQAAYEIGGRNQLFLFKDEKYWLINNLVPEPHY 372
Cdd:cd00094    6 PLSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGKNLEPGY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327537 373 PRSIHSLGFPASVKKIDAAVFDPLRQKVYFFVDKQYWRYDVRQELMDAAYPKLISTHFPGIRPKIDAVLYFKR-HYYIFQ 451
Cdd:cd00094   86 PKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDgYYYFFK 165

                        170       180
                 ....*....|....*....|....*....
gi 291327537 452 GAYQLEYDP--LLHRVTKTLSSTS-WFGC 477
Cdd:cd00094  166 GDQYWRFDPrsKEVRVGYPLKISSdWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 116-272 2.42e-30

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: 114.76  E-value: 2.42e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327537   116 RWMKRYLTYRIYnyTPDMKRaDVDYIFQKAFQVWSDVTPLRFRKIHkGEADITILFAFGDHGDFYdfdgkggtlAHAFYP 195
Cdd:smart00235   4 KWPKGTVPYVID--SSSLSP-EEREAIAKALAEWSDVTCIRFVERT-GTADIYISFGSGDSGCTL---------SHAGRP 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327537   196 GpgiqGDAHFDEaETWTKSFQgtnlflVAVHELGHSLGLPHSNNPKS---IMYPTYRYLHPNTFRLSADDIHSIQSLYGA 272
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 ...
 143-271 1.41e-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: 82.50  E-value: 1.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327537 143 QKAFQVWSDVTPLRFrkIHKGE----ADITILFafgdhGDFYDFDGKGGTLAHAFYPGPGIQGDA---HFDEAETWTKSF 215
Cdd:cd04279   27 KQAAAEWENVGPLKF--VYNPEedndADIVIFF-----DRPPPVGGAGGGLARAGFPLISDGNRKlfnRTDINLGPGQPR 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 291327537 216 QGTNLFLVAVHELGHSLGLPH-SNNPKSIMYPTYRYLHPNTFRLSADDIHSIQSLYG 271
Cdd:cd04279  100 GAENLQAIALHELGHALGLWHhSDRPEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 144-271 2.05e-15

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: 74.37  E-value: 2.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327537 144 KAFQVWSDVTPLRFRKI-HKGEADITIlfafgdhgdFYDFDGKGGTLAHAFYPGPGI----QGDAHFDEAETWTKSFQGT 218
Cdd:cd04277   41 DALEAWEDVADIDFVEVsDNSGADIRF---------GNSSDPDGNTAGYAYYPGSGSgtayGGDIWFNSSYDTNSDSPGS 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291327537 219 NLFLVAVHELGHSLGLPHS----------------NNPKSIM--------YPTYRYLHPNTFRLsaDDIHSIQSLYG 271
Cdd:cd04277  112 YGYQTIIHEIGHALGLEHPgdynggdpvpptyaldSREYTVMsynsgygnGASAGGGYPQTPML--LDIAALQYLYG 186
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 120-270 1.89e-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: 71.01  E-value: 1.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327537 120 RYLTYRIYNYTPDMK----RADVDYIFQKAFQVWSDVTPLRF--RKIHKGEADITILFAFGDHGdfydfdgkGGTLAHAF 193
Cdd:cd00203    1 KVIPYVVVADDRDVEeenlSAQIQSLILIAMQIWRDYLNIRFvlVGVEIDKADIAILVTRQDFD--------GGTGGWAY 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327537 194 YPG--PGIQGDAHFDEAETWTKSFqgtnlFLVAVHELGHSLGLPHSNNPK--------------------SIMYPTY-RY 250
Cdd:cd00203   73 LGRvcDSLRGVGVLQDNQSGTKEG-----AQTIAHELGHALGFYHDHDRKdrddyptiddtlnaedddyySVMSYTKgSF 147

                        170       180
                 ....*....|....*....|
gi 291327537 251 LHPNTFRLSADDIHSIQSLY 270
Cdd:cd00203  148 SDGQRKDFSQCDIDQINKLY 167
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 388-433 7.13e-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: 54.17  E-value: 7.13e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 291327537   388 IDAAVFDPlRQKVYFFVDKQYWRYDVRQelMDAAYPKLISTHFPGI 433
Cdd:smart00120   1 IDAAFELR-DGKTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGL 43
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 388-433 2.70e-08

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 49.87  E-value: 2.70e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 291327537  388 IDAAVFDPlRQKVYFFVDKQYWRYDVRQelMDAAYPKLIStHFPGI 433
Cdd:pfam00045   1 IDAAFEDR-DGKTYFFKGRKYWRFDPQR--VEPGYPKLIS-DFPGL 42
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 119-270 5.08e-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: 52.50  E-value: 5.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327537 119 KRYLTYRIYNYTPDMKRAdvdyIFQKAFQVWSDVTPLRFRKIHKG-EADITIlFAFGDhgdfydfdGKGGTLAHAFYPGp 197
Cdd:cd04268    1 KKPITYYIDDSVPDKLRA----AILDAIEAWNKAFAIGFKNANDVdPADIRY-SVIRW--------IPYNDGTWSYGPS- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327537 198 giqgDAHFDEAETWTKSFQGTNLFL---------VAVHELGHSLGLPHSNNPK----------------SIMYPTYRYLH 252
Cdd:cd04268   67 ----QVDPLTGEILLARVYLYSSFVeysgarlrnTAEHELGHALGLRHNFAASdrddnvdllaekgdtsSVMDYAPSNFS 142

                        170       180
                 ....*....|....*....|...
gi 291327537 253 PNTF-----RLSADDIHSIQSLY 270
Cdd:cd04268  143 IQLGdgqkyTIGPYDIAAIKKLY 165
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 142-274 1.75e-07

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 51.99  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327537 142 FQKAFQVWSDVtpLRFRKIHKGE-ADITILFA-----FGDHGDF--------YDFDGKGGTLAHAF--YPGPGiQGDahf 205
Cdd:COG5549  106 VLQAIAEWNAY--LPLEVVENPEnADIIIVRSnppltASPNPETgarsaettYEFYDTGNILSHRFtiLLSPN-QTG--- 179

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291327537 206 deaetwtKSFQGTnlflvAVHELGHSLGLP-HSNNPKSIMYP-TYRYLHPntfrLSADDIHSIQSLYGAPV 274
Cdd:COG5549  180 -------KYLLAT-----ARHELGHALGIWgHSPSPTDAMYFsQVRNPPP----ISPRDINTLKRIYQQPT 234
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 41-95 5.80e-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: 46.35  E-value: 5.80e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 291327537   41 AEWYLSRFFDYQGdripmTKTKTNRNLLEEKLQEMQQFFGLEVTGQLDTSTLKIM 95
Cdd:pfam01471   8 LQRYLNRLGYYPG-----PVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 340-382 1.64e-06

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 44.86  E-value: 1.64e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 291327537  340 IQAAYEIGgRNQLFLFKDEKYWLINNLVPEPHYPRSIHSL-GFP 382
Cdd:pfam00045   1 IDAAFEDR-DGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLP 43
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
223-247 1.69e-05

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 45.33  E-value: 1.69e-05
                         10        20
                 ....*....|....*....|....*
gi 291327537 223 VAVHELGHSLGLPHSNNPKSIMYPT 247
Cdd:COG1913  126 EAVHELGHLFGLGHCPNPRCVMHFS 150
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
224-245 3.20e-05

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 44.15  E-value: 3.20e-05
                         10        20
                 ....*....|....*....|..
gi 291327537 224 AVHELGHSLGLPHSNNPKSIMY 245
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 340-382 1.14e-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: 39.53  E-value: 1.14e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 291327537   340 IQAAYEIGGrNQLFLFKDEKYWLINNLVPEPHYPRSIHSL--GFP 382
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDPKRVDPGYPKLISSFfpGLP 44
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 224-245 1.34e-04

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 42.70  E-value: 1.34e-04
                         10        20
                 ....*....|....*....|..
gi 291327537 224 AVHELGHSLGLPHSNNPKSIMY 245
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVMN 150
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 223-247 2.73e-04

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: 41.51  E-value: 2.73e-04
                         10        20
                 ....*....|....*....|....*
gi 291327537 223 VAVHELGHSLGLPHSNNPKSIMYPT 247
Cdd:cd11375  126 EAVHELGHLFGLDHCPYYACVMNFS 150
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 221-265 3.20e-03

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


Pssm-ID: 239801  Cd Length: 207  Bit Score: 38.76  E-value: 3.20e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 291327537 221 FLVAvHELGHSLGLPH---------SNNPKSIMYPTyryLHPNTFRL-----SADDIHS 265
Cdd:cd04273  142 FTIA-HELGHVLGMPHdgdgnscgpEGKDGHIMSPT---LGANTGPFtwskcSRRYLTS 196
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 146-266 7.13e-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: 7.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291327537 146 FQVWsDVTPLRFRKIHkgeaDITILFAFGDHgdFYDFDGKG--GTLAHAFYpGPGIQGDAHfdeaetwtksfqgTNLFLV 223
Cdd:cd04269   73 FLDW-KRSNLLPRKPH----DNAQLLTGRDF--DGNTVGLAyvGGMCSPKY-SGGVVQDHS-------------RNLLLF 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 291327537 224 AV---HELGHSLGLPHSNN------PKSIMYPtYRYLHPNTF-RLSADDIHSI 266
Cdd:cd04269  132 AVtmaHELGHNLGMEHDDGgctcgrSTCIMAP-SPSSLTDAFsNCSYEDYQKF 183
 
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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