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Conserved domains on  [gi|2519850563|ref|NP_034939|]
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stromelysin-1 preproprotein [Mus musculus]

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 ...
 108-264 9.67e-94

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: 280.66  E-value: 9.67e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563 108 KWRKSHITYRIVNYTPDLPRQSVDSAIEKALKVWEEVTPLTFSRISEGEADIMISFAVGEHGDFVPFDGPGTVLAHAYAP 187
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563 188 GPGINGDAHFDDDERWTEDVT---GTNLFLVAAHELGHSLGLYHSAKAEALMYPVYkSSTDLSRFHLSQDDVDGIQSLYG 264
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDpphGINLFLVAAHEIGHALGLGHSSDPGAIMYPTY-SPLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 290-477 2.21e-80

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: 247.61  E-value: 2.21e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563 290 CSStLFFDAVSTLRGEVLFFKDRHFWRKSLRTPEPEFYLISSFWPSLPSNMDAAYEVTNRDTVFIFKGNQFWAIRGHEEL 369
Cdd:cd00094     4 CDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGKNLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563 370 AGYPKSIHTLGLPATVKKIDAAISNKEKRKTYFFVEDKYWRFDEKKQSMEPGFPRKIAEDFPGVDSRVDAVFEAF-GFLY 448
Cdd:cd00094    83 PGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLdGYYY 162

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2519850563 449 FFSGSSQLEFDPNAKK--VTHILKSNS-WFNC 477
Cdd:cd00094   163 FFKGDQYWRFDPRSKEvrVGYPLKISSdWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 32-87 1.06e-05

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: 42.89  E-value: 1.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2519850563  32 ELLQKYLENYYGLAKDvkqfIKKKDSSLIVKKIQEMQKFLGLEMTGKLDSNTMELM 87
Cdd:pfam01471   6 KELQRYLNRLGYYPGP----VDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 108-264 9.67e-94

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: 280.66  E-value: 9.67e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563 108 KWRKSHITYRIVNYTPDLPRQSVDSAIEKALKVWEEVTPLTFSRISEGEADIMISFAVGEHGDFVPFDGPGTVLAHAYAP 187
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563 188 GPGINGDAHFDDDERWTEDVT---GTNLFLVAAHELGHSLGLYHSAKAEALMYPVYkSSTDLSRFHLSQDDVDGIQSLYG 264
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDpphGINLFLVAAHEIGHALGLGHSSDPGAIMYPTY-SPLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 290-477 2.21e-80

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: 247.61  E-value: 2.21e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563 290 CSStLFFDAVSTLRGEVLFFKDRHFWRKSLRTPEPEFYLISSFWPSLPSNMDAAYEVTNRDTVFIFKGNQFWAIRGHEEL 369
Cdd:cd00094     4 CDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGKNLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563 370 AGYPKSIHTLGLPATVKKIDAAISNKEKRKTYFFVEDKYWRFDEKKQSMEPGFPRKIAEDFPGVDSRVDAVFEAF-GFLY 448
Cdd:cd00094    83 PGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLdGYYY 162

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2519850563 449 FFSGSSQLEFDPNAKK--VTHILKSNS-WFNC 477
Cdd:cd00094   163 FFKGDQYWRFDPRSKEvrVGYPLKISSdWLGC 194
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 108-264 3.82e-80

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


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 245.58  E-value: 3.82e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563 108 KWRKSHITYRIVNYTPDLPRQSVDSAIEKALKVWEEVTPLTFSRI-SEGEADIMISFAVGEHGDFVPFDGPGTVLAHAYA 186
Cdd:cd04278     1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563 187 PGpGINGDAHFDDDERWTE--DVTGTNLFLVAAHELGHSLGLYHSAKAEALMYPVYKSSTdlSRFHLSQDDVDGIQSLYG 264
Cdd:cd04278    81 PG-GIGGDIHFDDDEQWTLgsDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV--PKFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 105-264 4.30e-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: 132.86  E-value: 4.30e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563  105 GSPKWRKSHITYRIvnYTPDLPRqSVDSAIEKALKVWEEVTPLTFSRISeGEADIMISFAVGEHGDFvpfdgpgtvLAHA 184
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVERT-GTADIYISFGSGDSGCT---------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563  185 YAPGpginGDAHFDDdERWTEDVTgtnlflVAAHELGHSLGLYHSAKAEA---LMYPVYKSStDLSRFHLSQDDVDGIQS 261
Cdd:smart00235  68 GRPG----GDQHLSL-GNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNI-DTRNFDLSEDDSLGIPY 135


                   ...
gi 2519850563  262 LYG 264
Cdd:smart00235 136 DYG 138
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 388-435 4.55e-10

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 54.94  E-value: 4.55e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2519850563  388 IDAAISNKEkRKTYFFVEDKYWRFDEkkQSMEPGFPRKIAEDFPGVDS 435
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 388-432 4.95e-08

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 49.10  E-value: 4.95e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2519850563 388 IDAAISNKEKrKTYFFVEDKYWRFDEKKqsMEPGFPRKIAeDFPG 432
Cdd:pfam00045   1 IDAAFEDRDG-KTYFFKGRKYWRFDPQR--VEPGYPKLIS-DFPG 41
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 32-87 1.06e-05

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: 42.89  E-value: 1.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2519850563  32 ELLQKYLENYYGLAKDvkqfIKKKDSSLIVKKIQEMQKFLGLEMTGKLDSNTMELM 87
Cdd:pfam01471   6 KELQRYLNRLGYYPGP----VDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 108-264 9.67e-94

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: 280.66  E-value: 9.67e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563 108 KWRKSHITYRIVNYTPDLPRQSVDSAIEKALKVWEEVTPLTFSRISEGEADIMISFAVGEHGDFVPFDGPGTVLAHAYAP 187
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563 188 GPGINGDAHFDDDERWTEDVT---GTNLFLVAAHELGHSLGLYHSAKAEALMYPVYkSSTDLSRFHLSQDDVDGIQSLYG 264
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDpphGINLFLVAAHEIGHALGLGHSSDPGAIMYPTY-SPLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 290-477 2.21e-80

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: 247.61  E-value: 2.21e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563 290 CSStLFFDAVSTLRGEVLFFKDRHFWRKSLRTPEPEFYLISSFWPSLPSNMDAAYEVTNRDTVFIFKGNQFWAIRGHEEL 369
Cdd:cd00094     4 CDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGKNLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563 370 AGYPKSIHTLGLPATVKKIDAAISNKEKRKTYFFVEDKYWRFDEKKQSMEPGFPRKIAEDFPGVDSRVDAVFEAF-GFLY 448
Cdd:cd00094    83 PGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLdGYYY 162

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2519850563 449 FFSGSSQLEFDPNAKK--VTHILKSNS-WFNC 477
Cdd:cd00094   163 FFKGDQYWRFDPRSKEvrVGYPLKISSdWLGC 194
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 108-264 3.82e-80

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


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 245.58  E-value: 3.82e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563 108 KWRKSHITYRIVNYTPDLPRQSVDSAIEKALKVWEEVTPLTFSRI-SEGEADIMISFAVGEHGDFVPFDGPGTVLAHAYA 186
Cdd:cd04278     1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563 187 PGpGINGDAHFDDDERWTE--DVTGTNLFLVAAHELGHSLGLYHSAKAEALMYPVYKSSTdlSRFHLSQDDVDGIQSLYG 264
Cdd:cd04278    81 PG-GIGGDIHFDDDEQWTLgsDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV--PKFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 105-264 4.30e-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: 132.86  E-value: 4.30e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563  105 GSPKWRKSHITYRIvnYTPDLPRqSVDSAIEKALKVWEEVTPLTFSRISeGEADIMISFAVGEHGDFvpfdgpgtvLAHA 184
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVERT-GTADIYISFGSGDSGCT---------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563  185 YAPGpginGDAHFDDdERWTEDVTgtnlflVAAHELGHSLGLYHSAKAEA---LMYPVYKSStDLSRFHLSQDDVDGIQS 261
Cdd:smart00235  68 GRPG----GDQHLSL-GNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNI-DTRNFDLSEDDSLGIPY 135


                   ...
gi 2519850563  262 LYG 264
Cdd:smart00235 136 DYG 138
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 114-263 3.61e-17

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: 78.72  E-value: 3.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563 114 ITYRIVNYTPDLPRQS----VDSAIEKALKVWEEVTPLTF--SRISEGEADIMISFAvgeHGDFvpfDGPGtvLAHAYAP 187
Cdd:cd00203     3 IPYVVVADDRDVEEENlsaqIQSLILIAMQIWRDYLNIRFvlVGVEIDKADIAILVT---RQDF---DGGT--GGWAYLG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563 188 G--PGINGDAHFDDDERWTEDVtgtnlFLVAAHELGHSLGLYHSAKAEA--------------------LMYPVYKSSTD 245
Cdd:cd00203    75 RvcDSLRGVGVLQDNQSGTKEG-----AQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKGSFSD 149

                         170
                  ....*....|....*...
gi 2519850563 246 LSRFHLSQDDVDGIQSLY 263
Cdd:cd00203   150 GQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 128-264 1.01e-14

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: 71.33  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563 128 QSVDSAIEKALKVWEEVTPLTFSRISEGE--ADIMISFavgehGDFVPFDGPGTVLAHAYAPGpgingDAHFDDDERWTE 205
Cdd:cd04279    20 QSWLQAVKQAAAEWENVGPLKFVYNPEEDndADIVIFF-----DRPPPVGGAGGGLARAGFPL-----ISDGNRKLFNRT 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2519850563 206 DV--------TGTNLFLVAAHELGHSLGLYH-SAKAEALMYPVYkSSTDLSRFHLSQDDVDGIQSLYG 264
Cdd:cd04279    90 DInlgpgqprGAENLQAIALHELGHALGLWHhSDRPEDAMYPSQ-GQGPDGNPTLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 132-264 4.95e-13

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


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 67.44  E-value: 4.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563 132 SAIEKALKVWEEVTPLTFSRISEGE-ADIMISFavgehgdfvpFDGP-GTVLAHAYAPGPGIN----GDAHFDDDERWTE 205
Cdd:cd04277    37 AAARDALEAWEDVADIDFVEVSDNSgADIRFGN----------SSDPdGNTAGYAYYPGSGSGtaygGDIWFNSSYDTNS 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563 206 DVTGTNLFLVAAHELGHSLGLYHSAKAEA----------------LM-YPVYKSSTDLSRFHLSQ----DDVDGIQSLYG 264
Cdd:cd04277   107 DSPGSYGYQTIIHEIGHALGLEHPGDYNGgdpvpptyaldsreytVMsYNSGYGNGASAGGGYPQtpmlLDIAALQYLYG 186
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 114-263 2.43e-12

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


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 64.83  E-value: 2.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563 114 ITYRIVNYTPDlprqSVDSAIEKALKVWEEVTPLTFS-RISEGEADIMISFavgeHGDFVPFDGPGTVLAHAYAPGpgiN 192
Cdd:cd04268     4 ITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKnANDVDPADIRYSV----IRWIPYNDGTWSYGPSQVDPL---T 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563 193 GDAHFDDDERWTEDV--TGTNLFLVAAHELGHSLGLYHSAKA----------------EALMYP----VYKSSTDLSRFH 250
Cdd:cd04268    73 GEILLARVYLYSSFVeySGARLRNTAEHELGHALGLRHNFAAsdrddnvdllaekgdtSSVMDYapsnFSIQLGDGQKYT 152

                         170
                  ....*....|...
gi 2519850563 251 LSQDDVDGIQSLY 263
Cdd:cd04268   153 IGPYDIAAIKKLY 165
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 388-435 4.55e-10

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 54.94  E-value: 4.55e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2519850563  388 IDAAISNKEkRKTYFFVEDKYWRFDEkkQSMEPGFPRKIAEDFPGVDS 435
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 388-432 4.95e-08

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 49.10  E-value: 4.95e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2519850563 388 IDAAISNKEKrKTYFFVEDKYWRFDEKKqsMEPGFPRKIAeDFPG 432
Cdd:pfam00045   1 IDAAFEDRDG-KTYFFKGRKYWRFDPQR--VEPGYPKLIS-DFPG 41
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 296-338 1.18e-07

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: 48.01  E-value: 1.18e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2519850563  296 FDAVSTLR-GEVLFFKDRHFWRKSLRTPEPEF-YLISSFWPSLPS 338
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDPGYpKLISSFFPGLPC 45
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 32-87 1.06e-05

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: 42.89  E-value: 1.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2519850563  32 ELLQKYLENYYGLAKDvkqfIKKKDSSLIVKKIQEMQKFLGLEMTGKLDSNTMELM 87
Cdd:pfam01471   6 KELQRYLNRLGYYPGP----VDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 296-338 1.78e-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: 41.78  E-value: 1.78e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2519850563 296 FDAVSTLR-GEVLFFKDRHFWRKSLRTPEPEF-YLISSFwPSLPS 338
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVEPGYpKLISDF-PGLPC 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 341-382 4.10e-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: 40.63  E-value: 4.10e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2519850563 341 DAAYEVtNRDTVFIFKGNQFWAIRGHEELAGYPKSIHTL-GLP 382
Cdd:pfam00045   2 DAAFED-RDGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 341-382 7.54e-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: 39.92  E-value: 7.54e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2519850563  341 DAAYEVtNRDTVFIFKGNQFWAIRGHEELAGYPKSIHTL--GLP 382
Cdd:smart00120   2 DAAFEL-RDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFfpGLP 44
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 178-264 1.03e-03

Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ADAM family of metalloproteases contains proteolytic domains from snake venoms, proteases from the mammalian reproductive tract, and the tumor necrosis factor alpha convertase, TACE. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239795  Cd Length: 192  Bit Score: 40.10  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519850563 178 GTVLAHAYAPGPGINGDahfddDERWTEDvTGTNLF--LVAAHELGHSLGLYHSAKAEA----------LMYPVyksSTD 245
Cdd:cd04267   103 GDILGLAYVGSMCNPYS-----SVGVVED-TGFTLLtaLTMAHELGHNLGAEHDGGDELafecdgggnyIMAPV---DSG 173

                          90
                  ....*....|....*....
gi 2519850563 246 LSRFHLSQDDVDGIQSLYG 264
Cdd:cd04267   174 LNSYRFSQCSIGSIREFLD 192
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 437-477 5.15e-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: 34.85  E-value: 5.15e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2519850563 437 VDAVFEAF-GFLYFFSGSSQLEFDPN-AKKVTHILKSNS-WFNC 477
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQrVEPGYPKLISDFpGLPC 44
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 200-240 6.01e-03

Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239803  Cd Length: 197  Bit Score: 38.08  E-value: 6.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2519850563 200 DERWTEDVTGTNLFLVAAHELGHSLGLYHSAKAEAlMYPVY 240
Cdd:cd04276   104 DQLWYEDLLAASLRYLLAHEVGHTLGLRHNFKASS-DGSNE 143
DUF4953 pfam16313
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ...
 215-239 6.76e-03

Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic met-zincin mmotif HExxHxxGxxH, the extended zinc-binding domain of metallopeptidases.


Pssm-ID: 435269  Cd Length: 319  Bit Score: 38.39  E-value: 6.76e-03
                          10        20
                  ....*....|....*....|....*
gi 2519850563 215 VAAHELGHSLGLYHSAKAEAlMYPV 239
Cdd:pfam16313  16 VSAHEVGHTLGLRHNFAASS-AYPV 39
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 210-228 9.66e-03

Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 37.21  E-value: 9.66e-03
                          10        20
                  ....*....|....*....|..
gi 2519850563 210 TNLFLVA---AHELGHSLGLYH 228
Cdd:cd04269   126 RNLLLFAvtmAHELGHNLGMEH 147
 
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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