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Conserved domains on  [gi|560879435|ref|NP_001274067|]
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macrophage metalloelastase precursor [Canis lupus familiaris]

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 ...
 110-264 1.80e-93

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: 279.89  E-value: 1.80e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435  110 WKKHLITYRINNYTPDMQPADVDYAIHKAFEVWSNVTPLKFRKVNSGEADIMILFASRAHGDFSPFDGRGGVIAHAFGPG 189
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFPG 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 560879435  190 PQIGGDMHFDEAEIWTK---TYKGTNLFLVAVHELGHSLGLGHSSDPKAIMFPTYSYVNPNTFHLSADDIHGIQSLYG 264
Cdd:pfam00413  82 PGLGGDIHFDDDETWTVgsdPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 282-455 2.19e-73

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: 229.51  E-value: 2.19e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435 282 NCDSnLSFDAVTTVGNKIFFFKDRFLWWRHPESPKNSVTLISSLWPTLPSGIQAAYEIGARNQVFLFKDDKYWLISNLRP 361
Cdd:cd00094    3 ACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGKNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435 362 QPHYPKNIHSLGFPDSVKKIDAAVFNPLLYKTYFFVDDQFWRYDEKTQFMDPGYPKLITKYFPGIKPTVDAVYYYNR-HY 440
Cdd:cd00094   82 EPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDgYY 161

                        170
                 ....*....|....*
gi 560879435 441 YFFQGPDVFEYDVIS 455
Cdd:cd00094  162 YFFKGDQYWRFDPRS 176
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 29-88 3.09e-10

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: 55.60  E-value: 3.09e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435   29 NDVASSQRYLeNFYGFvmdgIPKTKMGVGGNLMENKIQEMQQFLGLKVTGKLDASTLDMM 88
Cdd:pfam01471   3 EDVKELQRYL-NRLGY----YPGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 110-264 1.80e-93

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: 279.89  E-value: 1.80e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435  110 WKKHLITYRINNYTPDMQPADVDYAIHKAFEVWSNVTPLKFRKVNSGEADIMILFASRAHGDFSPFDGRGGVIAHAFGPG 189
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFPG 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 560879435  190 PQIGGDMHFDEAEIWTK---TYKGTNLFLVAVHELGHSLGLGHSSDPKAIMFPTYSYVNPNTFHLSADDIHGIQSLYG 264
Cdd:pfam00413  82 PGLGGDIHFDDDETWTVgsdPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 110-264 4.62e-80

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 245.19  E-value: 4.62e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435 110 WKKHLITYRINNYTPDMQPADVDYAIHKAFEVWSNVTPLKFRKVNSG-EADIMILFASRAHGDFSPFDGRGGVIAHAFGP 188
Cdd:cd04278    2 WSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFFP 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 560879435 189 GPqIGGDMHFDEAEIWTKT--YKGTNLFLVAVHELGHSLGLGHSSDPKAIMFPTYSYVNPNtFHLSADDIHGIQSLYG 264
Cdd:cd04278   82 GG-IGGDIHFDDDEQWTLGsdSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK-FKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 282-455 2.19e-73

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: 229.51  E-value: 2.19e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435 282 NCDSnLSFDAVTTVGNKIFFFKDRFLWWRHPESPKNSVTLISSLWPTLPSGIQAAYEIGARNQVFLFKDDKYWLISNLRP 361
Cdd:cd00094    3 ACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGKNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435 362 QPHYPKNIHSLGFPDSVKKIDAAVFNPLLYKTYFFVDDQFWRYDEKTQFMDPGYPKLITKYFPGIKPTVDAVYYYNR-HY 440
Cdd:cd00094   82 EPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDgYY 161

                        170
                 ....*....|....*
gi 560879435 441 YFFQGPDVFEYDVIS 455
Cdd:cd00094  162 YFFKGDQYWRFDPRS 176
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 106-264 1.38e-33

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: 123.23  E-value: 1.38e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435   106 GRPVWKKHLITYRInnYTPDMQPaDVDYAIHKAFEVWSNVTPLKFRKVNSGeADIMILFASRAHGDFspfdgrggvIAHA 185
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDSGCT---------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435   186 FGPGpqigGDMHFDEaeiwtktYKGTNLFLVAVHELGHSLGLGHSSDPKA---IMFPTYSYVNPNTFHLSADDIHGIQSL 262
Cdd:smart00235  68 GRPG----GDQHLSL-------GNGCINTGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136


                   ..
gi 560879435   263 YG 264
Cdd:smart00235 137 YG 138
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 381-426 5.01e-11

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 57.64  E-value: 5.01e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 560879435   381 IDAAVFNPLLyKTYFFVDDQFWRYDEKTqfMDPGYPKLITKYFPGI 426
Cdd:smart00120   1 IDAAFELRDG-KTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGL 43
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 29-88 3.09e-10

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: 55.60  E-value: 3.09e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435   29 NDVASSQRYLeNFYGFvmdgIPKTKMGVGGNLMENKIQEMQQFLGLKVTGKLDASTLDMM 88
Cdd:pfam01471   3 EDVKELQRYL-NRLGY----YPGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 381-426 2.99e-09

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 52.57  E-value: 2.99e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 560879435  381 IDAAVFNPLlYKTYFFVDDQFWRYDEKTqfMDPGYPKLITKyFPGI 426
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQR--VEPGYPKLISD-FPGL 42
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 134-263 2.68e-07

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 51.61  E-value: 2.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435 134 AIHKAFEVWSNVTPLKfrKVNSGE-ADIMILFaSRAHGDFSPFDGRGGVIAHAfGPGPQIGGDMHFDEAEIWTK-TYKGT 211
Cdd:COG5549  105 AVLQAIAEWNAYLPLE--VVENPEnADIIIVR-SNPPLTASPNPETGARSAET-TYEFYDTGNILSHRFTILLSpNQTGK 180

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 560879435 212 NLFLVAVHELGHSLGL-GHSSDPKAIMFPtySYV-NPNTfhLSADDIHGIQSLY 263
Cdd:COG5549  181 YLLATARHELGHALGIwGHSPSPTDAMYF--SQVrNPPP--ISPRDINTLKRIY 230
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
217-238 5.97e-05

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 43.38  E-value: 5.97e-05
                         10        20
                 ....*....|....*....|..
gi 560879435 217 AVHELGHSLGLGHSSDPKAIMF 238
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 217-237 3.81e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 38.46  E-value: 3.81e-03
                         10        20
                 ....*....|....*....|.
gi 560879435 217 AVHELGHSLGLGHSSDPKAIM 237
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 ...
 110-264 1.80e-93

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: 279.89  E-value: 1.80e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435  110 WKKHLITYRINNYTPDMQPADVDYAIHKAFEVWSNVTPLKFRKVNSGEADIMILFASRAHGDFSPFDGRGGVIAHAFGPG 189
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFPG 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 560879435  190 PQIGGDMHFDEAEIWTK---TYKGTNLFLVAVHELGHSLGLGHSSDPKAIMFPTYSYVNPNTFHLSADDIHGIQSLYG 264
Cdd:pfam00413  82 PGLGGDIHFDDDETWTVgsdPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 110-264 4.62e-80

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 245.19  E-value: 4.62e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435 110 WKKHLITYRINNYTPDMQPADVDYAIHKAFEVWSNVTPLKFRKVNSG-EADIMILFASRAHGDFSPFDGRGGVIAHAFGP 188
Cdd:cd04278    2 WSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFFP 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 560879435 189 GPqIGGDMHFDEAEIWTKT--YKGTNLFLVAVHELGHSLGLGHSSDPKAIMFPTYSYVNPNtFHLSADDIHGIQSLYG 264
Cdd:cd04278   82 GG-IGGDIHFDDDEQWTLGsdSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK-FKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 282-455 2.19e-73

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: 229.51  E-value: 2.19e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435 282 NCDSnLSFDAVTTVGNKIFFFKDRFLWWRHPESPKNSVTLISSLWPTLPSGIQAAYEIGARNQVFLFKDDKYWLISNLRP 361
Cdd:cd00094    3 ACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGKNL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435 362 QPHYPKNIHSLGFPDSVKKIDAAVFNPLLYKTYFFVDDQFWRYDEKTQFMDPGYPKLITKYFPGIKPTVDAVYYYNR-HY 440
Cdd:cd00094   82 EPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDgYY 161

                        170
                 ....*....|....*
gi 560879435 441 YFFQGPDVFEYDVIS 455
Cdd:cd00094  162 YFFKGDQYWRFDPRS 176
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 106-264 1.38e-33

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: 123.23  E-value: 1.38e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435   106 GRPVWKKHLITYRInnYTPDMQPaDVDYAIHKAFEVWSNVTPLKFRKVNSGeADIMILFASRAHGDFspfdgrggvIAHA 185
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDSGCT---------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435   186 FGPGpqigGDMHFDEaeiwtktYKGTNLFLVAVHELGHSLGLGHSSDPKA---IMFPTYSYVNPNTFHLSADDIHGIQSL 262
Cdd:smart00235  68 GRPG----GDQHLSL-------GNGCINTGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136


                   ..
gi 560879435   263 YG 264
Cdd:smart00235 137 YG 138
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 134-264 3.63e-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: 84.05  E-value: 3.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435 134 AIHKAFEVWSNVTPLKFRKV--NSGEADIMILFASRAHGDfspfdGRGGVIAHAFGPGPQIGGDMHFDEAEIW---TKTY 208
Cdd:cd04279   25 AVKQAAAEWENVGPLKFVYNpeEDNDADIVIFFDRPPPVG-----GAGGGLARAGFPLISDGNRKLFNRTDINlgpGQPR 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 560879435 209 KGTNLFLVAVHELGHSLGLGHSSD-PKAIMFPTYSYVNPNTFHLSADDIHGIQSLYG 264
Cdd:cd04279  100 GAENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 134-264 1.79e-13

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: 68.60  E-value: 1.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435 134 AIHKAFEVWSNVTPLKFRKVNSGE-ADIMILFASRAHGDfspfdgrggVIAHAFGPGPQI----GGDMHFDEAEIWTKTY 208
Cdd:cd04277   38 AARDALEAWEDVADIDFVEVSDNSgADIRFGNSSDPDGN---------TAGYAYYPGSGSgtayGGDIWFNSSYDTNSDS 108

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 560879435 209 KGTNLFLVAVHELGHSLGLGHS-----SDPKAIMFP---------TY--SYVNPNTFH------LSADDIHGIQSLYG 264
Cdd:cd04277  109 PGSYGYQTIIHEIGHALGLEHPgdyngGDPVPPTYAldsreytvmSYnsGYGNGASAGggypqtPMLLDIAALQYLYG 186
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 115-263 2.91e-13

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: 67.55  E-value: 2.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435 115 ITYRI----NNYTPDMQPADVDYAIHKAFEVWSNVTPLKFRKVNSGE--ADIMILFASRAHGdfspfdgrGGVIAHAFGP 188
Cdd:cd00203    3 IPYVVvaddRDVEEENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIdkADIAILVTRQDFD--------GGTGGWAYLG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435 189 GPQ--IGGDMHFDEAEIWTKTYKGTnlflvAVHELGHSLGLGHSSDPKA--------------------IMFPTY-SYVN 245
Cdd:cd00203   75 RVCdsLRGVGVLQDNQSGTKEGAQT-----IAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKgSFSD 149

                        170
                 ....*....|....*...
gi 560879435 246 PNTFHLSADDIHGIQSLY 263
Cdd:cd00203  150 GQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 115-263 5.39e-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: 64.05  E-value: 5.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435 115 ITYRINNYTPDmqpaDVDYAIHKAFEVWSNVTPLKFRKVNSG-EADIMILFASRAHGDFSpfdgrggviAHAFGPG--PQ 191
Cdd:cd04268    4 ITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNANDVdPADIRYSVIRWIPYNDG---------TWSYGPSqvDP 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435 192 IGGDMHFDEAEIWTKTYKGTNLFL--VAVHELGHSLGLGHSSDPKA----------------IMFPTYSYVNPNTF---- 249
Cdd:cd04268   71 LTGEILLARVYLYSSFVEYSGARLrnTAEHELGHALGLRHNFAASDrddnvdllaekgdtssVMDYAPSNFSIQLGdgqk 150

                        170
                 ....*....|....*
gi 560879435 250 -HLSADDIHGIQSLY 263
Cdd:cd04268  151 yTIGPYDIAAIKKLY 165
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 381-426 5.01e-11

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 57.64  E-value: 5.01e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 560879435   381 IDAAVFNPLLyKTYFFVDDQFWRYDEKTqfMDPGYPKLITKYFPGI 426
Cdd:smart00120   1 IDAAFELRDG-KTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGL 43
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 29-88 3.09e-10

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: 55.60  E-value: 3.09e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435   29 NDVASSQRYLeNFYGFvmdgIPKTKMGVGGNLMENKIQEMQQFLGLKVTGKLDASTLDMM 88
Cdd:pfam01471   3 EDVKELQRYL-NRLGY----YPGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 381-426 2.99e-09

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 52.57  E-value: 2.99e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 560879435  381 IDAAVFNPLlYKTYFFVDDQFWRYDEKTqfMDPGYPKLITKyFPGI 426
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQR--VEPGYPKLISD-FPGL 42
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 333-375 1.58e-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: 47.56  E-value: 1.58e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 560879435  333 IQAAYEIGaRNQVFLFKDDKYWLISNLRPQPHYPKNIHSL-GFP 375
Cdd:pfam00045   1 IDAAFEDR-DGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLP 43
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 134-263 2.68e-07

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 51.61  E-value: 2.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435 134 AIHKAFEVWSNVTPLKfrKVNSGE-ADIMILFaSRAHGDFSPFDGRGGVIAHAfGPGPQIGGDMHFDEAEIWTK-TYKGT 211
Cdd:COG5549  105 AVLQAIAEWNAYLPLE--VVENPEnADIIIVR-SNPPLTASPNPETGARSAET-TYEFYDTGNILSHRFTILLSpNQTGK 180

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 560879435 212 NLFLVAVHELGHSLGL-GHSSDPKAIMFPtySYV-NPNTfhLSADDIHGIQSLY 263
Cdd:COG5549  181 YLLATARHELGHALGIwGHSPSPTDAMYF--SQVrNPPP--ISPRDINTLKRIY 230
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 333-375 2.74e-06

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: 44.16  E-value: 2.74e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 560879435   333 IQAAYEIGaRNQVFLFKDDKYWLISNLRPQPHYPKNIHSL--GFP 375
Cdd:smart00120   1 IDAAFELR-DGKTYFFKGDKYWRFDPKRVDPGYPKLISSFfpGLP 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 289-331 1.67e-05

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: 41.84  E-value: 1.67e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 560879435   289 FDAVTTVGN-KIFFFKDRFLWWRHPESP-KNSVTLISSLWPTLPS 331
Cdd:smart00120   1 IDAAFELRDgKTYFFKGDKYWRFDPKRVdPGYPKLISSFFPGLPC 45
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
217-238 5.97e-05

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 43.38  E-value: 5.97e-05
                         10        20
                 ....*....|....*....|..
gi 560879435 217 AVHELGHSLGLGHSSDPKAIMF 238
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
216-240 6.07e-05

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 43.41  E-value: 6.07e-05
                         10        20
                 ....*....|....*....|....*
gi 560879435 216 VAVHELGHSLGLGHSSDPKAIMFPT 240
Cdd:COG1913  126 EAVHELGHLFGLGHCPNPRCVMHFS 150
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 216-242 1.55e-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: 42.28  E-value: 1.55e-04
                         10        20
                 ....*....|....*....|....*..
gi 560879435 216 VAVHELGHSLGLGHSSDPKAIMFPTYS 242
Cdd:cd11375  126 EAVHELGHLFGLDHCPYYACVMNFSNS 152
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 110-229 7.21e-04

Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family contain two conserved disulphide bridges, these are joined 1-4 and 2-3. Members of this family have an amino terminal propeptide which is cleaved to give the active protease domain. All other linked domains are found to the carboxyl terminus of this domain. This family includes: Astacin, a digestive enzyme from Crayfish. Meprin, a multiple domain membrane component that is constructed from a homologous alpha and beta chain. Proteins involved in morphogenesis such as Swiss:P13497, and Tolloid from drosophila.


Pssm-ID: 426242 [Multi-domain]  Cd Length: 192  Bit Score: 40.73  E-value: 7.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 560879435  110 WKKHLITYRI-NNYTPDMQPAdvdyaIHKAFEVWSNVTPLKFrKVNSGEADIMILFASRAHGDFSpFDGRGGviahafgp 188
Cdd:pfam01400   3 WPNGPIPYVIdGSLTGLARAL-----IRQAMRHWENKTCIRF-VERTPAPDNNYLFFFKGDGCYS-YVGRVG-------- 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 560879435  189 GPQ---IGgdmhfdeaeiwtktyKGTNLFLVAVHELGHSLGLGH 229
Cdd:pfam01400  68 GRQpvsIG---------------DGCDKFGIIVHELGHALGFFH 96
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 289-331 8.28e-04

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: 37.16  E-value: 8.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 560879435  289 FDAVTTVG-NKIFFFKDRFLWWRHPESP-KNSVTLISSlWPTLPS 331
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVePGYPKLISD-FPGLPC 44
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 217-237 3.81e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 38.46  E-value: 3.81e-03
                         10        20
                 ....*....|....*....|.
gi 560879435 217 AVHELGHSLGLGHSSDPKAIM 237
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVM 149
 
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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