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Conserved domains on  [gi|73858572|ref|NP_002417|]
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macrophage metalloelastase preproprotein [Homo sapiens]

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 ...
109-263 4.33e-97

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


:

Pssm-ID: 395334  Cd Length: 159  Bit Score: 288.75  E-value: 4.33e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572   109 WRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDFHAFDGKGGILAHAFGPG 188
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFPG 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 73858572   189 SGIGGDAHFDEDEFWTTHSG---GTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDIRGIQSLYG 263
Cdd:pfam00413  82 PGLGGDIHFDDDETWTVGSDpphGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
279-470 4.19e-83

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: 254.54  E-value: 4.19e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572 279 PALCDPnLSFDAVTTVGNKIFFFKDRFFWLKVSERPKTSVNLISSLWPTLPSGIEAAYEIEARNQVFLFKDDKYWLISNL 358
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572 359 RPEPNYPKSIHSFGFPNFVKKIDAAVFNPRFYRTYFFVDNQYWRYDERRQMMDPGYPKLITKNFQGIGPKIDAVFYSKNK 438
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDG 159
                       170       180       190
                ....*....|....*....|....*....|....*
gi 73858572 439 YYYFFQGSNQFEYDF--LLQRITKTLKSNS-WFGC 470
Cdd:cd00094 160 YYYFFKGDQYWRFDPrsKEVRVGYPLKISSdWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
28-87 1.30e-08

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


:

Pssm-ID: 396175 [Multi-domain]  Cd Length: 57  Bit Score: 50.98  E-value: 1.30e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572    28 NNVLFGERYLEKFYGLEInklPVTKmkYSGNLMKEKIQEMQHFLGLKVTGQLDTSTLEMM 87
Cdd:pfam01471   3 EDVKELQRYLARLGYYSG---PVDG--YFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
109-263 4.33e-97

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 395334  Cd Length: 159  Bit Score: 288.75  E-value: 4.33e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572   109 WRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDFHAFDGKGGILAHAFGPG 188
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFPG 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 73858572   189 SGIGGDAHFDEDEFWTTHSG---GTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDIRGIQSLYG 263
Cdd:pfam00413  82 PGLGGDIHFDDDETWTVGSDpphGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
279-470 4.19e-83

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: 254.54  E-value: 4.19e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572 279 PALCDPnLSFDAVTTVGNKIFFFKDRFFWLKVSERPKTSVNLISSLWPTLPSGIEAAYEIEARNQVFLFKDDKYWLISNL 358
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572 359 RPEPNYPKSIHSFGFPNFVKKIDAAVFNPRFYRTYFFVDNQYWRYDERRQMMDPGYPKLITKNFQGIGPKIDAVFYSKNK 438
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDG 159
                       170       180       190
                ....*....|....*....|....*....|....*
gi 73858572 439 YYYFFQGSNQFEYDF--LLQRITKTLKSNS-WFGC 470
Cdd:cd00094 160 YYYFFKGDQYWRFDPrsKEVRVGYPLKISSdWLGC 194
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
109-263 1.31e-81

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: 249.04  E-value: 1.31e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572 109 WRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGM-ADILVVFARGAHGDFHAFDGKGGILAHAFGP 187
Cdd:cd04278   2 WSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISFARGNHGDGYPFDGPGGTLAHAFFP 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 73858572 188 GsGIGGDAHFDEDEFWTTHS--GGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDiNTFRLSADDIRGIQSLYG 263
Cdd:cd04278  82 G-GIGGDIHFDDDEQWTLGSdsGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV-PKFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
105-263 5.56e-37

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: 132.47  E-value: 5.56e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572    105 GGPVWRKHYITYRInnYTPDMNReDVDYAIRKAFQVWSNVTPLKFSKiNTGMADILVVFARGAHGDFhafdgkggiLAHA 184
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVE-RTGTADIYISFGSGDSGCT---------LSHA 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572    185 FGPGsgigGDAHFDeDEFWTTHSGgtnlflTAVHEIGHSLGLGHSSDPKA---VMFPTYKYVDINTFRLSADDIRGIQSL 261
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136

                   ..
gi 73858572    262 YG 263
Cdd:smart00235 137 YG 138
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
380-427 8.62e-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: 56.87  E-value: 8.62e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 73858572    380 IDAAVFNPRFYrTYFFVDNQYWRYDERRqmMDPGYPKLITKNFQGIGP 427
Cdd:smart00120   1 IDAAFELRDGK-TYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
380-427 2.05e-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  Cd Length: 44  Bit Score: 52.95  E-value: 2.05e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 73858572   380 IDAAVFNPRfYRTYFFVDNQYWRYDERRqmMDPGYPKLITkNFQGIGP 427
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQR--VEPGYPKLIS-DFPGLPC 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
28-87 1.30e-08

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


Pssm-ID: 396175 [Multi-domain]  Cd Length: 57  Bit Score: 50.98  E-value: 1.30e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572    28 NNVLFGERYLEKFYGLEInklPVTKmkYSGNLMKEKIQEMQHFLGLKVTGQLDTSTLEMM 87
Cdd:pfam01471   3 EDVKELQRYLARLGYYSG---PVDG--YFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
216-237 2.09e-05

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 411395  Cd Length: 170  Bit Score: 44.92  E-value: 2.09e-05
                         10        20
                 ....*....|....*....|..
gi 73858572  216 AVHEIGHSLGLGHSSDPKAVMF 237
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
216-245 5.28e-04

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 40.78  E-value: 5.28e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 73858572  216 AVHEIGHSLGLGHSSDPKAVMF--PTYKYVDI 245
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVMNfsNSVRDVDI 160
Zn_serralysin NF035945
serralysin family metalloprotease;
135-263 1.87e-03

serralysin family metalloprotease;


Pssm-ID: 411534 [Multi-domain]  Cd Length: 457  Bit Score: 40.34  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572  135 RKAFQVWSNVTPLKFSKI-NTGMADIlvvfargahgDFHAFDGKGGilAHAFGPGS-GIGGDAHF-DEDEFWTTHSGGTN 211
Cdd:NF035945  86 KLSLQSWSDVANITFTEVsAGQKANI----------TFGNYSDSGQ--AYAYLPGTsDVSGQSWYnYNSDYIRNLTPDLG 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572  212 LF--LTAVHEIGHSLGLGHSSDPKAVM-FPTYKYV----DINTFRL------------------SA---DDIRGIQSLYG 263
Cdd:NF035945 154 NYgrQTLTHEIGHTLGLSHPGDYNAGEgNPTYKDAtyaeDTRQYSVmsywsesntgqdfkghyaSApllDDIAAIQKLYG 233
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
216-238 2.08e-03

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


Pssm-ID: 224825  Cd Length: 181  Bit Score: 38.90  E-value: 2.08e-03
                        10        20
                ....*....|....*....|...
gi 73858572 216 AVHEIGHSLGLGHSSDPKAVMFP 238
Cdd:COG1913 128 VLHELGHLLGLSHCPNPRCVMNF 150
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
109-263 4.33e-97

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 395334  Cd Length: 159  Bit Score: 288.75  E-value: 4.33e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572   109 WRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDFHAFDGKGGILAHAFGPG 188
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFPG 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 73858572   189 SGIGGDAHFDEDEFWTTHSG---GTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDIRGIQSLYG 263
Cdd:pfam00413  82 PGLGGDIHFDDDETWTVGSDpphGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
279-470 4.19e-83

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: 254.54  E-value: 4.19e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572 279 PALCDPnLSFDAVTTVGNKIFFFKDRFFWLKVSERPKTSVNLISSLWPTLPSGIEAAYEIEARNQVFLFKDDKYWLISNL 358
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572 359 RPEPNYPKSIHSFGFPNFVKKIDAAVFNPRFYRTYFFVDNQYWRYDERRQMMDPGYPKLITKNFQGIGPKIDAVFYSKNK 438
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDG 159
                       170       180       190
                ....*....|....*....|....*....|....*
gi 73858572 439 YYYFFQGSNQFEYDF--LLQRITKTLKSNS-WFGC 470
Cdd:cd00094 160 YYYFFKGDQYWRFDPrsKEVRVGYPLKISSdWLGC 194
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
109-263 1.31e-81

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: 249.04  E-value: 1.31e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572 109 WRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGM-ADILVVFARGAHGDFHAFDGKGGILAHAFGP 187
Cdd:cd04278   2 WSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISFARGNHGDGYPFDGPGGTLAHAFFP 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 73858572 188 GsGIGGDAHFDEDEFWTTHS--GGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDiNTFRLSADDIRGIQSLYG 263
Cdd:cd04278  82 G-GIGGDIHFDDDEQWTLGSdsGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV-PKFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
105-263 5.56e-37

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: 132.47  E-value: 5.56e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572    105 GGPVWRKHYITYRInnYTPDMNReDVDYAIRKAFQVWSNVTPLKFSKiNTGMADILVVFARGAHGDFhafdgkggiLAHA 184
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVE-RTGTADIYISFGSGDSGCT---------LSHA 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572    185 FGPGsgigGDAHFDeDEFWTTHSGgtnlflTAVHEIGHSLGLGHSSDPKA---VMFPTYKYVDINTFRLSADDIRGIQSL 261
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136

                   ..
gi 73858572    262 YG 263
Cdd:smart00235 137 YG 138
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
133-263 4.47e-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: 83.66  E-value: 4.47e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572 133 AIRKAFQVWSNVTPLKFSKINTGM--ADILVVFARGAHGDfhafdGKGGILAHAFGPGSGIGGDAHFDEDEFWTTH---S 207
Cdd:cd04279  25 AVKQAAAEWENVGPLKFVYNPEEDndADIVIFFDRPPPVG-----GAGGGLARAGFPLISDGNRKLFNRTDINLGPgqpR 99
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 73858572 208 GGTNLFLTAVHEIGHSLGLGHSSD-PKAVMFPTYKYVDINTFRLSADDIRGIQSLYG 263
Cdd:cd04279 100 GAENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
133-263 9.77e-17

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  Cd Length: 186  Bit Score: 78.23  E-value: 9.77e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572 133 AIRKAFQVWSNVTPLKFSKI-NTGMADILVVFARGAHGDFHAFdgkggilahAFGPGSGI----GGDAHFDEDEFWTTHS 207
Cdd:cd04277  38 AARDALEAWEDVADIDFVEVsDNSGADIRFGNSSDPDGNTAGY---------AYYPGSGSgtayGGDIWFNSSYDTNSDS 108
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 73858572 208 GGTNLFLTAVHEIGHSLGLGHSSDPKA----------------VM----FPTYKYVDINTF--RLSADDIRGIQSLYG 263
Cdd:cd04277 109 PGSYGYQTIIHEIGHALGLEHPGDYNGgdpvpptyaldsreytVMsynsGYGNGASAGGGYpqTPMLLDIAALQYLYG 186
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
113-262 2.41e-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: 67.93  E-value: 2.41e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572 113 YITYRI----NNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGM--ADILVVFARGAHGdfhafdgkGGILAHAFG 186
Cdd:cd00203   2 VIPYVVvaddRDVEEENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIdkADIAILVTRQDFD--------GGTGGWAYL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572 187 PGS--GIGGDAHFDEDEFWTThsggtNLFLTAVHEIGHSLGLGHSSDPKA--------------------VMFPTY-KYV 243
Cdd:cd00203  74 GRVcdSLRGVGVLQDNQSGTK-----EGAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKgSFS 148
                       170
                ....*....|....*....
gi 73858572 244 DINTFRLSADDIRGIQSLY 262
Cdd:cd00203 149 DGQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
114-262 1.03e-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: 65.98  E-value: 1.03e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572 114 ITYRINNYTPDMNREdvdyAIRKAFQVWSNVTPLKFSKINTGM-ADILVVFARGAHGDfhafDGKGGILAHAFGPGSGig 192
Cdd:cd04268   4 ITYYIDDSVPDKLRA----AILDAIEAWNKAFAIGFKNANDVDpADIRYSVIRWIPYN----DGTWSYGPSQVDPLTG-- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572 193 gDAHFDEDEFWTTHSGGTNLFL--TAVHEIGHSLGLGHSSDPKA----------------VMFPTYKYVDINTF-----R 249
Cdd:cd04268  74 -EILLARVYLYSSFVEYSGARLrnTAEHELGHALGLRHNFAASDrddnvdllaekgdtssVMDYAPSNFSIQLGdgqkyT 152
                       170
                ....*....|...
gi 73858572 250 LSADDIRGIQSLY 262
Cdd:cd04268 153 IGPYDIAAIKKLY 165
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
380-427 8.62e-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: 56.87  E-value: 8.62e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 73858572    380 IDAAVFNPRFYrTYFFVDNQYWRYDERRqmMDPGYPKLITKNFQGIGP 427
Cdd:smart00120   1 IDAAFELRDGK-TYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
380-427 2.05e-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  Cd Length: 44  Bit Score: 52.95  E-value: 2.05e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 73858572   380 IDAAVFNPRfYRTYFFVDNQYWRYDERRqmMDPGYPKLITkNFQGIGP 427
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQR--VEPGYPKLIS-DFPGLPC 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
28-87 1.30e-08

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


Pssm-ID: 396175 [Multi-domain]  Cd Length: 57  Bit Score: 50.98  E-value: 1.30e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572    28 NNVLFGERYLEKFYGLEInklPVTKmkYSGNLMKEKIQEMQHFLGLKVTGQLDTSTLEMM 87
Cdd:pfam01471   3 EDVKELQRYLARLGYYSG---PVDG--YFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
332-375 6.90e-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  Cd Length: 44  Bit Score: 48.33  E-value: 6.90e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 73858572   332 IEAAYEIEaRNQVFLFKDDKYWLISNLRPEPNYPKSIHSF-GFPN 375
Cdd:pfam00045   1 IDAAFEDR-DGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLPC 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
332-376 2.15e-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: 2.15e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 73858572    332 IEAAYEIEaRNQVFLFKDDKYWLISNLRPEPNYPKSIHSFgFPNF 376
Cdd:smart00120   1 IDAAFELR-DGKTYFFKGDKYWRFDPKRVDPGYPKLISSF-FPGL 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
288-330 1.01e-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: 42.61  E-value: 1.01e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 73858572    288 FDAVTTVGN-KIFFFKDRFFWLKVSERP-KTSVNLISSLWPTLPS 330
Cdd:smart00120   1 IDAAFELRDgKTYFFKGDKYWRFDPKRVdPGYPKLISSFFPGLPC 45
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
216-237 2.09e-05

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 411395  Cd Length: 170  Bit Score: 44.92  E-value: 2.09e-05
                         10        20
                 ....*....|....*....|..
gi 73858572  216 AVHEIGHSLGLGHSSDPKAVMF 237
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
215-239 8.14e-05

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: 43.05  E-value: 8.14e-05
                        10        20
                ....*....|....*....|....*
gi 73858572 215 TAVHEIGHSLGLGHSSDPKAVMFPT 239
Cdd:cd11375 126 EAVHELGHLFGLDHCPYYACVMNFS 150
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
429-470 2.43e-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  Cd Length: 44  Bit Score: 38.32  E-value: 2.43e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 73858572   429 IDAVFYSKNKYYYFFQGSNQFEYDFL-LQRITKTLKSNS-WFGC 470
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQrVEPGYPKLISDFpGLPC 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
429-469 2.60e-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: 2.60e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 73858572    429 IDAVFYSKNKYYYFFQGSNQFEYDF-LLQRITKTLKSNSWFG 469
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPkRVDPGYPKLISSFFPG 42
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
216-245 5.28e-04

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 40.78  E-value: 5.28e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 73858572  216 AVHEIGHSLGLGHSSDPKAVMF--PTYKYVDI 245
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVMNfsNSVRDVDI 160
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
288-330 1.72e-03

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  Cd Length: 44  Bit Score: 36.01  E-value: 1.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 73858572   288 FDAVTTVG-NKIFFFKDRFFWLKVSERP-KTSVNLISSlWPTLPS 330
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVePGYPKLISD-FPGLPC 44
Zn_serralysin NF035945
serralysin family metalloprotease;
135-263 1.87e-03

serralysin family metalloprotease;


Pssm-ID: 411534 [Multi-domain]  Cd Length: 457  Bit Score: 40.34  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572  135 RKAFQVWSNVTPLKFSKI-NTGMADIlvvfargahgDFHAFDGKGGilAHAFGPGS-GIGGDAHF-DEDEFWTTHSGGTN 211
Cdd:NF035945  86 KLSLQSWSDVANITFTEVsAGQKANI----------TFGNYSDSGQ--AYAYLPGTsDVSGQSWYnYNSDYIRNLTPDLG 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572  212 LF--LTAVHEIGHSLGLGHSSDPKAVM-FPTYKYV----DINTFRL------------------SA---DDIRGIQSLYG 263
Cdd:NF035945 154 NYgrQTLTHEIGHTLGLSHPGDYNAGEgNPTYKDAtyaeDTRQYSVmsywsesntgqdfkghyaSApllDDIAAIQKLYG 233
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
216-238 2.08e-03

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


Pssm-ID: 224825  Cd Length: 181  Bit Score: 38.90  E-value: 2.08e-03
                        10        20
                ....*....|....*....|...
gi 73858572 216 AVHEIGHSLGLGHSSDPKAVMFP 238
Cdd:COG1913 128 VLHELGHLLGLSHCPNPRCVMNF 150
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
111-229 8.66e-03

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteristic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 404470  Cd Length: 122  Bit Score: 36.18  E-value: 8.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572   111 KHYITYRINNyTPDMNReDVDYAIRKAFQVWSNVtplkfskINTGMADILVVFARgahgdfHAFDGKGGIlahAFGPGSG 190
Cdd:pfam13582  25 VAIIITTSAD-DPYTTS-DALEILDENQQVIDTR-------IGQYGYDLGHLFTT------RDFGGGGGL---AYVGGVC 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 73858572   191 IGGDAhfdedeF---WTTHSGGTNLFLTAVHEIGHSLGLGHS 229
Cdd:pfam13582  87 NSGSK------FgvnYGSSPVGDTGVDTFAHEIGHNFGLNHT 122
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
133-228 9.86e-03

Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239819 [Multi-domain]  Cd Length: 198  Bit Score: 37.36  E-value: 9.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73858572 133 AIRKAFQVWSNVTPLKFSKINTGMADILVVFARGaHGDFHAFdGKGGILAHAFGPGSGIGGDAHFDEDEFWTThsggtnl 212
Cdd:cd04327  24 KVRAAAREWLPYANLKFKFVTDADADIRISFTPG-DGYWSYV-GTDALLIGADAPTMNLGWFTDDTPDPEFSR------- 94
                        90
                ....*....|....*.
gi 73858572 213 flTAVHEIGHSLGLGH 228
Cdd:cd04327  95 --VVLHEFGHALGFIH 108
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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