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Conserved domains on  [gi|45359865|ref|NP_004762|]
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matrix metalloproteinase-20 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 ...
 116-271 4.15e-95

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


:

Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 284.51  E-value: 4.15e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865   116 KWKKNTLTYRISKYTPSMSSVEVDKAVEMALQAWSSAVPLSFVRINSGEADIMISFENGDHGDSYPFDGPRGTLAHAFAP 195
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45359865   196 GEGLGGDTHFDNAEKWTMGT---NGFNLFTVAAHEFGHALGLAHSTDPSALMYPTYKYKNPYGFHLPKDDVKGIQALYG 271
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSdppHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 293-483 2.90e-65

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: 209.09  E-value: 2.90e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 293 PDLCDSSSsFDAVTMLGKELLLFKDRIFWRRQVHLRtGIRPSTITSSFPQLMSNVDAAYEVAERGTAYFFKGPHYWITRG 372
Cdd:cd00094   1 PDACDPLS-FDAVTTLRGELYFFKGRYFWRLSPGKP-PGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 373 FQMQ-GPPRTIYDFGFPRHVQQIDAAVYLREPQKTLFFVGDEYYSYDERKRKMEKDYPKNTEEEFSGVNGQIDAAVE-LN 450
Cdd:cd00094  79 KNLEpGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLD 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 45359865 451 GYIYFFSGPKTYKYDT---EKEDVVSVVKSSSWIGC 483
Cdd:cd00094 159 GYYYFFKGDQYWRFDPrskEVRVGYPLKISSDWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 35-95 5.19e-06

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: 43.66  E-value: 5.19e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45359865    35 RNNYRLAQAYLDKYytnkeGHQIGEMVARGSNSMIRKIKELQAFFGLQVTGKLDQTTMNVI 95
Cdd:pfam01471   2 GEDVKELQRYLNRL-----GYYPGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 116-271 4.15e-95

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


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 284.51  E-value: 4.15e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865   116 KWKKNTLTYRISKYTPSMSSVEVDKAVEMALQAWSSAVPLSFVRINSGEADIMISFENGDHGDSYPFDGPRGTLAHAFAP 195
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45359865   196 GEGLGGDTHFDNAEKWTMGT---NGFNLFTVAAHEFGHALGLAHSTDPSALMYPTYKYKNPYGFHLPKDDVKGIQALYG 271
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSdppHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 116-271 1.52e-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: 247.12  E-value: 1.52e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 116 KWKKNTLTYRISKYTPSMSSVEVDKAVEMALQAWSSAVPLSFVRINSG-EADIMISFENGDHGDSYPFDGPRGTLAHAFA 194
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45359865 195 PGeGLGGDTHFDNAEKWTMGTN--GFNLFTVAAHEFGHALGLAHSTDPSALMYPTYKYKNPyGFHLPKDDVKGIQALYG 271
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLGSDsgGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 293-483 2.90e-65

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: 209.09  E-value: 2.90e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 293 PDLCDSSSsFDAVTMLGKELLLFKDRIFWRRQVHLRtGIRPSTITSSFPQLMSNVDAAYEVAERGTAYFFKGPHYWITRG 372
Cdd:cd00094   1 PDACDPLS-FDAVTTLRGELYFFKGRYFWRLSPGKP-PGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 373 FQMQ-GPPRTIYDFGFPRHVQQIDAAVYLREPQKTLFFVGDEYYSYDERKRKMEKDYPKNTEEEFSGVNGQIDAAVE-LN 450
Cdd:cd00094  79 KNLEpGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLD 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 45359865 451 GYIYFFSGPKTYKYDT---EKEDVVSVVKSSSWIGC 483
Cdd:cd00094 159 GYYYFFKGDQYWRFDPrskEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 113-272 1.58e-39

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: 139.41  E-value: 1.58e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865    113 GEPKWKKNTLTYRIskYTPSMSSvEVDKAVEMALQAWSSAVPLSFVRiNSGEADIMISFENGDHGdsyPFdgprgtLAHA 192
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVE-RTGTADIYISFGSGDSG---CT------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865    193 FAPGeglgGDTHFDNaEKWTMGTNgfnlftVAAHEFGHALGLAHSTDPSA---LMYPTYKYKNPYGFHLPKDDVKGIQAL 269
Cdd:smart00235  68 GRPG----GDQHLSL-GNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136


                   ...
gi 45359865    270 YGP 272
Cdd:smart00235 137 YGS 139
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 140-246 1.97e-06

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 48.91  E-value: 1.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 140 KAVEMALQAWSSAVPLSFVRiNSGEADIMISFENGDHGDSyPFDGPRGTLAHAfapgeglggDTHFDNAEKWTM------ 213
Cdd:COG5549 104 AAVLQAIAEWNAYLPLEVVE-NPENADIIIVRSNPPLTAS-PNPETGARSAET---------TYEFYDTGNILShrftil 172

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 45359865 214 -GTNGFNLFTVAA--HEFGHALGL-AHSTDPSALMYP 246
Cdd:COG5549 173 lSPNQTGKYLLATarHELGHALGIwGHSPSPTDAMYF 209
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 347-389 4.17e-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: 43.77  E-value: 4.17e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 45359865    347 VDAAYEVaERGTAYFFKGPHYWITRGFQMQ-GPPRTIYDF--GFPR 389
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDPKRVDpGYPKLISSFfpGLPC 45
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 35-95 5.19e-06

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: 43.66  E-value: 5.19e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45359865    35 RNNYRLAQAYLDKYytnkeGHQIGEMVARGSNSMIRKIKELQAFFGLQVTGKLDQTTMNVI 95
Cdd:pfam01471   2 GEDVKELQRYLNRL-----GYYPGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 347-388 2.86e-05

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 41.40  E-value: 2.86e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 45359865   347 VDAAYEVaERGTAYFFKGPHYWITRGFQMQ-GPPRTIYDF-GFP 388
Cdd:pfam00045   1 IDAAFED-RDGKTYFFKGRKYWRFDPQRVEpGYPKLISDFpGLP 43
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 116-271 4.15e-95

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


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 284.51  E-value: 4.15e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865   116 KWKKNTLTYRISKYTPSMSSVEVDKAVEMALQAWSSAVPLSFVRINSGEADIMISFENGDHGDSYPFDGPRGTLAHAFAP 195
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45359865   196 GEGLGGDTHFDNAEKWTMGT---NGFNLFTVAAHEFGHALGLAHSTDPSALMYPTYKYKNPYGFHLPKDDVKGIQALYG 271
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSdppHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 116-271 1.52e-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: 247.12  E-value: 1.52e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 116 KWKKNTLTYRISKYTPSMSSVEVDKAVEMALQAWSSAVPLSFVRINSG-EADIMISFENGDHGDSYPFDGPRGTLAHAFA 194
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45359865 195 PGeGLGGDTHFDNAEKWTMGTN--GFNLFTVAAHEFGHALGLAHSTDPSALMYPTYKYKNPyGFHLPKDDVKGIQALYG 271
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLGSDsgGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 293-483 2.90e-65

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: 209.09  E-value: 2.90e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 293 PDLCDSSSsFDAVTMLGKELLLFKDRIFWRRQVHLRtGIRPSTITSSFPQLMSNVDAAYEVAERGTAYFFKGPHYWITRG 372
Cdd:cd00094   1 PDACDPLS-FDAVTTLRGELYFFKGRYFWRLSPGKP-PGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 373 FQMQ-GPPRTIYDFGFPRHVQQIDAAVYLREPQKTLFFVGDEYYSYDERKRKMEKDYPKNTEEEFSGVNGQIDAAVE-LN 450
Cdd:cd00094  79 KNLEpGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLD 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 45359865 451 GYIYFFSGPKTYKYDT---EKEDVVSVVKSSSWIGC 483
Cdd:cd00094 159 GYYYFFKGDQYWRFDPrskEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 113-272 1.58e-39

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: 139.41  E-value: 1.58e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865    113 GEPKWKKNTLTYRIskYTPSMSSvEVDKAVEMALQAWSSAVPLSFVRiNSGEADIMISFENGDHGdsyPFdgprgtLAHA 192
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVE-RTGTADIYISFGSGDSG---CT------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865    193 FAPGeglgGDTHFDNaEKWTMGTNgfnlftVAAHEFGHALGLAHSTDPSA---LMYPTYKYKNPYGFHLPKDDVKGIQAL 269
Cdd:smart00235  68 GRPG----GDQHLSL-GNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136


                   ...
gi 45359865    270 YGP 272
Cdd:smart00235 137 YGS 139
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 119-271 1.05e-16

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: 77.11  E-value: 1.05e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 119 KNTLTYRIS--KYTPSMSSVEVDKAVEMALQAWSSAVPLSFVRI--NSGEADIMISFengdhGDSYPFDGPRGTLAHAFA 194
Cdd:cd04279   1 KSPIRVYIDptPAPPDSRAQSWLQAVKQAAAEWENVGPLKFVYNpeEDNDADIVIFF-----DRPPPVGGAGGGLARAGF 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 195 PGEGLGGDTHFDNAEKW---TMGTNGFNLFTVAAHEFGHALGLAHSTD-PSALMYPTYKYKNPYGFHLPKDDVKGIQALY 270
Cdd:cd04279  76 PLISDGNRKLFNRTDINlgpGQPRGAENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVATLKRLY 155


                .
gi 45359865 271 G 271
Cdd:cd04279 156 G 156
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 120-270 3.81e-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: 67.16  E-value: 3.81e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 120 NTLTYRI----SKYTPSMSSVEVDKAVEMALQAWSSAVPLSFVRINSGE--ADIMISFENGDHgdsypfdgPRGTLAHAF 193
Cdd:cd00203   1 KVIPYVVvaddRDVEEENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIdkADIAILVTRQDF--------DGGTGGWAY 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 194 APG--EGLGGDTHFDnaekwTMGTNGFNLFTVAAHEFGHALGLAHSTDPSA--------------------LMYPTY-KY 250
Cdd:cd00203  73 LGRvcDSLRGVGVLQ-----DNQSGTKEGAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKgSF 147

                       170       180
                ....*....|....*....|
gi 45359865 251 KNPYGFHLPKDDVKGIQALY 270
Cdd:cd00203 148 SDGQRKDFSQCDIDQINKLY 167
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 140-271 1.83e-11

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: 62.82  E-value: 1.83e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 140 KAVEMALQAWSSAVPLSFVRINSGE-ADIMISFENGDHGDSYpfdgprgtlAHAFAPGEG----LGGDTHFDNAEKWTMG 214
Cdd:cd04277  37 AAARDALEAWEDVADIDFVEVSDNSgADIRFGNSSDPDGNTA---------GYAYYPGSGsgtaYGGDIWFNSSYDTNSD 107

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45359865 215 TNGFNLFTVAAHEFGHALGLAHS-----TDPSALMYP--TYKY-----------KNPYGFHLPK----DDVKGIQALYG 271
Cdd:cd04277 108 SPGSYGYQTIIHEIGHALGLEHPgdyngGDPVPPTYAldSREYtvmsynsgygnGASAGGGYPQtpmlLDIAALQYLYG 186
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 119-270 1.59e-09

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 56.74  E-value: 1.59e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 119 KNTLTYRISKYTPsmssVEVDKAVEMALQAWSSAVPLSFVRINSG-EADIMISFENgdhgdsypfDGPRGTLAHAFAPG- 196
Cdd:cd04268   1 KKPITYYIDDSVP----DKLRAAILDAIEAWNKAFAIGFKNANDVdPADIRYSVIR---------WIPYNDGTWSYGPSq 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 197 -EGLGGDTHFD--NAEKWTMGTNGFNLFTVAAHEFGHALGLAHS----------------TDPSALMYPT-----YKYKN 252
Cdd:cd04268  68 vDPLTGEILLArvYLYSSFVEYSGARLRNTAEHELGHALGLRHNfaasdrddnvdllaekGDTSSVMDYApsnfsIQLGD 147

                       170
                ....*....|....*...
gi 45359865 253 PYGFHLPKDDVKGIQALY 270
Cdd:cd04268 148 GQKYTIGPYDIAAIKKLY 165
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 138-236 1.02e-07

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: 52.38  E-value: 1.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 138 VDKAVEMAlQAWSSAVPLSFVRINSGEADIMISFENGDHGDSYpfdgprgtlahafapgegLGGDTHFDNAEKWTMGTNG 217
Cdd:cd04327  22 KDKVRAAA-REWLPYANLKFKFVTDADADIRISFTPGDGYWSY------------------VGTDALLIGADAPTMNLGW 82

                        90       100
                ....*....|....*....|....*.
gi 45359865 218 FNLFT-------VAAHEFGHALGLAH 236
Cdd:cd04327  83 FTDDTpdpefsrVVLHEFGHALGFIH 108
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 140-246 1.97e-06

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 48.91  E-value: 1.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359865 140 KAVEMALQAWSSAVPLSFVRiNSGEADIMISFENGDHGDSyPFDGPRGTLAHAfapgeglggDTHFDNAEKWTM------ 213
Cdd:COG5549 104 AAVLQAIAEWNAYLPLEVVE-NPENADIIIVRSNPPLTAS-PNPETGARSAET---------TYEFYDTGNILShrftil 172

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 45359865 214 -GTNGFNLFTVAA--HEFGHALGL-AHSTDPSALMYP 246
Cdd:COG5549 173 lSPNQTGKYLLATarHELGHALGIwGHSPSPTDAMYF 209
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 347-389 4.17e-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: 43.77  E-value: 4.17e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 45359865    347 VDAAYEVaERGTAYFFKGPHYWITRGFQMQ-GPPRTIYDF--GFPR 389
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDPKRVDpGYPKLISSFfpGLPC 45
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 35-95 5.19e-06

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: 43.66  E-value: 5.19e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45359865    35 RNNYRLAQAYLDKYytnkeGHQIGEMVARGSNSMIRKIKELQAFFGLQVTGKLDQTTMNVI 95
Cdd:pfam01471   2 GEDVKELQRYLNRL-----GYYPGPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 394-441 6.30e-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: 43.00  E-value: 6.30e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 45359865    394 IDAAVYLREpQKTLFFVGDEYYSYDErkRKMEKDYPKNTEEEFSGVNG 441
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 347-388 2.86e-05

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 41.40  E-value: 2.86e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 45359865   347 VDAAYEVaERGTAYFFKGPHYWITRGFQMQ-GPPRTIYDF-GFP 388
Cdd:pfam00045   1 IDAAFED-RDGKTYFFKGRKYWRFDPQRVEpGYPKLISDFpGLP 43
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
220-247 1.55e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 39.56  E-value: 1.55e-03
                        10        20
                ....*....|....*....|....*...
gi 45359865 220 LFTVAAHEFGHALGLAHSTDPSALMYPT 247
Cdd:COG1913 123 VLKEAVHELGHLFGLGHCPNPRCVMHFS 150
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 394-430 2.15e-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: 2.15e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 45359865   394 IDAAVYLRePQKTLFFVGDEYYSYDErkRKMEKDYPK 430
Cdd:pfam00045   1 IDAAFEDR-DGKTYFFKGRKYWRFDP--QRVEPGYPK 34
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 220-247 3.26e-03

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


Pssm-ID: 213029  Cd Length: 173  Bit Score: 38.43  E-value: 3.26e-03
                        10        20
                ....*....|....*....|....*...
gi 45359865 220 LFTVAAHEFGHALGLAHSTDPSALMYPT 247
Cdd:cd11375 123 LLKEAVHELGHLFGLDHCPYYACVMNFS 150
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 302-345 3.32e-03

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: 35.30  E-value: 3.32e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 45359865    302 FDAVTML-GKELLLFKDRIFWRRQVHLRTGIRPSTITSSFPQLMS 345
Cdd:smart00120   1 IDAAFELrDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 443-470 4.73e-03

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: 34.91  E-value: 4.73e-03
                           10        20
                   ....*....|....*....|....*....
gi 45359865    443 IDAAVEL-NGYIYFFSGPKTYKYDTEKED 470
Cdd:smart00120   1 IDAAFELrDGKTYFFKGDKYWRFDPKRVD 29
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 443-468 7.08e-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: 34.46  E-value: 7.08e-03
                          10        20
                  ....*....|....*....|....*..
gi 45359865   443 IDAAVEL-NGYIYFFSGPKTYKYDTEK 468
Cdd:pfam00045   1 IDAAFEDrDGKTYFFKGRKYWRFDPQR 27
 
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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