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Conserved domains on  [gi|85567332|gb|AAI12302|]
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Matrix metalloproteinase 12, 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 3.07e-97

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: 289.52  E-value: 3.07e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567332   109 WRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDFHAFDGKGGILAHAFGPG 188
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFPG 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 85567332   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 4.43e-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: 4.43e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567332 279 PALCDPnLSFDAVTTVGNKIFFFKDRFFWLKVSERPKTSVNLISSLWPTLPSGIEAAYEIEARNQVFLFKDDKYWLISNL 358
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567332 359 RPEPNYPKSIHSFGFPNFVKKIDAAVFNPRFYRTYFFVDNQYWRYDERRQMMDPGYPKLITKNFQGIGPKIDAVFYSKNK 438
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 85567332 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 1.39e-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: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 50.98  E-value: 1.39e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567332    28 NNVLFGERYLEKFYgleinKLPVTKMKYSGNLMKEKIQEMQHFLGLKVTGQLDTSTLEMM 87
Cdd:pfam01471   3 EDVKELQRYLNRLG-----YYPGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 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 3.07e-97

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: 289.52  E-value: 3.07e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567332   109 WRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDFHAFDGKGGILAHAFGPG 188
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFPG 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 85567332   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 4.43e-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: 4.43e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567332 279 PALCDPnLSFDAVTTVGNKIFFFKDRFFWLKVSERPKTSVNLISSLWPTLPSGIEAAYEIEARNQVFLFKDDKYWLISNL 358
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567332 359 RPEPNYPKSIHSFGFPNFVKKIDAAVFNPRFYRTYFFVDNQYWRYDERRQMMDPGYPKLITKNFQGIGPKIDAVFYSKNK 438
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 85567332 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 1.38e-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: 1.38e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567332 109 WRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGM-ADILVVFARGAHGDFHAFDGKGGILAHAFGP 187
Cdd:cd04278   2 WSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISFARGNHGDGYPFDGPGGTLAHAFFP 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 85567332 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 5.87e-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: 5.87e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567332    105 GGPVWRKHYITYRInnYTPDMNReDVDYAIRKAFQVWSNVTPLKFSKiNTGMADILVVFARGAHGDFhafdgkggiLAHA 184
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVE-RTGTADIYISFGSGDSGCT---------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567332    185 FGPGsgigGDAHFDeDEFWTTHSGgtnlflTAVHEIGHSLGLGHSSDPKA---VMFPTYKYVDINTFRLSADDIRGIQSL 261
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136


                   ..
gi 85567332    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 9.10e-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: 9.10e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 85567332    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 2.17e-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: 52.95  E-value: 2.17e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 85567332   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 1.39e-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: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 50.98  E-value: 1.39e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567332    28 NNVLFGERYLEKFYgleinKLPVTKMKYSGNLMKEKIQEMQHFLGLKVTGQLDTSTLEMM 87
Cdd:pfam01471   3 EDVKELQRYLNRLG-----YYPGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 133-249 5.50e-07

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 50.45  E-value: 5.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567332 133 AIRKAFQVWSNVTPLKFSKiNTGMADILVVFAR---GAHGDFHA----------FDGKGGILAHAF----GPgsgiggda 195
Cdd:COG5549 105 AVLQAIAEWNAYLPLEVVE-NPENADIIIVRSNpplTASPNPETgarsaettyeFYDTGNILSHRFtillSP-------- 175

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 85567332 196 hfdedefwttHSGGTNLFLTAVHEIGHSLGL-GHSSDPKAVMFP----TYKYV---DINTFR 249
Cdd:COG5549 176 ----------NQTGKYLLATARHELGHALGIwGHSPSPTDAMYFsqvrNPPPIsprDINTLK 227
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
216-237 2.19e-05

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 44.92  E-value: 2.19e-05
                         10        20
                 ....*....|....*....|..
gi 85567332  216 AVHEIGHSLGLGHSSDPKAVMF 237
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 216-245 5.58e-04

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 40.78  E-value: 5.58e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 85567332  216 AVHEIGHSLGLGHSSDPKAVMF--PTYKYVDI 245
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVMNfsNSVRDVDI 160
 
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 3.07e-97

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: 289.52  E-value: 3.07e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567332   109 WRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDFHAFDGKGGILAHAFGPG 188
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFPG 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 85567332   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 4.43e-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: 4.43e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567332 279 PALCDPnLSFDAVTTVGNKIFFFKDRFFWLKVSERPKTSVNLISSLWPTLPSGIEAAYEIEARNQVFLFKDDKYWLISNL 358
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567332 359 RPEPNYPKSIHSFGFPNFVKKIDAAVFNPRFYRTYFFVDNQYWRYDERRQMMDPGYPKLITKNFQGIGPKIDAVFYSKNK 438
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 85567332 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 1.38e-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: 1.38e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567332 109 WRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGM-ADILVVFARGAHGDFHAFDGKGGILAHAFGP 187
Cdd:cd04278   2 WSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISFARGNHGDGYPFDGPGGTLAHAFFP 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 85567332 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 5.87e-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: 5.87e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567332    105 GGPVWRKHYITYRInnYTPDMNReDVDYAIRKAFQVWSNVTPLKFSKiNTGMADILVVFARGAHGDFhafdgkggiLAHA 184
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVE-RTGTADIYISFGSGDSGCT---------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567332    185 FGPGsgigGDAHFDeDEFWTTHSGgtnlflTAVHEIGHSLGLGHSSDPKA---VMFPTYKYVDINTFRLSADDIRGIQSL 261
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136


                   ..
gi 85567332    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 4.72e-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: 4.72e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567332 133 AIRKAFQVWSNVTPLKFSKINTGM--ADILVVFARGAHGDfhafdGKGGILAHAFGPGSGIGGDAHFDEDEFWTTH---S 207
Cdd:cd04279  25 AVKQAAAEWENVGPLKFVYNPEEDndADIVIFFDRPPPVG-----GAGGGLARAGFPLISDGNRKLFNRTDINLGPgqpR 99

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 85567332 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 1.03e-16

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


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 78.23  E-value: 1.03e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567332 133 AIRKAFQVWSNVTPLKFSKI-NTGMADILVVFARGAHGDFHAFdgkggilahAFGPGSGI----GGDAHFDEDEFWTTHS 207
Cdd:cd04277  38 AARDALEAWEDVADIDFVEVsDNSGADIRFGNSSDPDGNTAGY---------AYYPGSGSgtayGGDIWFNSSYDTNSDS 108

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 85567332 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 2.55e-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: 2.55e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567332 113 YITYRI----NNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGM--ADILVVFARGAHGdfhafdgkGGILAHAFG 186
Cdd:cd00203   2 VIPYVVvaddRDVEEENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIdkADIAILVTRQDFD--------GGTGGWAYL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567332 187 PGS--GIGGDAHFDEDEFWTThsggtNLFLTAVHEIGHSLGLGHSSDPKA--------------------VMFPTY-KYV 243
Cdd:cd00203  74 GRVcdSLRGVGVLQDNQSGTK-----EGAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKgSFS 148

                       170
                ....*....|....*....
gi 85567332 244 DINTFRLSADDIRGIQSLY 262
Cdd:cd00203 149 DGQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 114-262 1.09e-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: 1.09e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567332 114 ITYRINNYTPDMNREdvdyAIRKAFQVWSNVTPLKFSKINTGM-ADILVVFARGAHGDfhafDGKGGILAHAFGPGSGig 192
Cdd:cd04268   4 ITYYIDDSVPDKLRA----AILDAIEAWNKAFAIGFKNANDVDpADIRYSVIRWIPYN----DGTWSYGPSQVDPLTG-- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567332 193 gDAHFDEDEFWTTHSGGTNLFL--TAVHEIGHSLGLGHSSDPKA----------------VMFPTYKYVDINTF-----R 249
Cdd:cd04268  74 -EILLARVYLYSSFVEYSGARLrnTAEHELGHALGLRHNFAASDrddnvdllaekgdtssVMDYAPSNFSIQLGdgqkyT 152

                       170
                ....*....|...
gi 85567332 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 9.10e-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: 9.10e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 85567332    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 2.17e-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: 52.95  E-value: 2.17e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 85567332   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 1.39e-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: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 50.98  E-value: 1.39e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567332    28 NNVLFGERYLEKFYgleinKLPVTKMKYSGNLMKEKIQEMQHFLGLKVTGQLDTSTLEMM 87
Cdd:pfam01471   3 EDVKELQRYLNRLG-----YYPGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 332-375 7.28e-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: 48.33  E-value: 7.28e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 85567332   332 IEAAYEIEaRNQVFLFKDDKYWLISNLRPEPNYPKSIHSF-GFPN 375
Cdd:pfam00045   1 IDAAFEDR-DGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLPC 44
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 133-249 5.50e-07

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 50.45  E-value: 5.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85567332 133 AIRKAFQVWSNVTPLKFSKiNTGMADILVVFAR---GAHGDFHA----------FDGKGGILAHAF----GPgsgiggda 195
Cdd:COG5549 105 AVLQAIAEWNAYLPLEVVE-NPENADIIIVRSNpplTASPNPETgarsaettyeFYDTGNILSHRFtillSP-------- 175

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 85567332 196 hfdedefwttHSGGTNLFLTAVHEIGHSLGL-GHSSDPKAVMFP----TYKYV---DINTFR 249
Cdd:COG5549 176 ----------NQTGKYLLATARHELGHALGIwGHSPSPTDAMYFsqvrNPPPIsprDINTLK 227
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 332-376 2.27e-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: 2.27e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 85567332    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 1.06e-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: 1.06e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 85567332    288 FDAVTTVGN-KIFFFKDRFFWLKVSERP-KTSVNLISSLWPTLPS 330
Cdd:smart00120   1 IDAAFELRDgKTYFFKGDKYWRFDPKRVdPGYPKLISSFFPGLPC 45
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
216-239 1.40e-05

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 45.33  E-value: 1.40e-05
                        10        20
                ....*....|....*....|....
gi 85567332 216 AVHEIGHSLGLGHSSDPKAVMFPT 239
Cdd:COG1913 127 AVHELGHLFGLGHCPNPRCVMHFS 150
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
216-237 2.19e-05

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 44.92  E-value: 2.19e-05
                         10        20
                 ....*....|....*....|..
gi 85567332  216 AVHEIGHSLGLGHSSDPKAVMF 237
Cdd:NF033823 126 AVHELGHLLGLGHCPNPRCVMH 147
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 215-239 8.59e-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: 8.59e-05
                        10        20
                ....*....|....*....|....*
gi 85567332 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 2.57e-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: 38.32  E-value: 2.57e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 85567332   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 2.75e-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: 2.75e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 85567332    429 IDAVFYSKNKYYYFFQGSNQFEYDF-LLQRITKTLKSNSWFG 469
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPkRVDPGYPKLISSFFPG 42
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 216-245 5.58e-04

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 40.78  E-value: 5.58e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 85567332  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 1.82e-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 [Multi-domain]  Cd Length: 44  Bit Score: 36.01  E-value: 1.82e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 85567332   288 FDAVTTVG-NKIFFFKDRFFWLKVSERP-KTSVNLISSlWPTLPS 330
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVePGYPKLISD-FPGLPC 44
 
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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