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Conserved domains on  [gi|46854939|gb|AAH69716|]
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Matrix metallopeptidase 3 (stromelysin 1, progelatinase) [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 ...
 108-264 1.72e-96

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: 287.59  E-value: 1.72e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939   108 KWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAP 187
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939   188 GPGINGDAHFDDDEQWTKDTT---GTNLFLVAAHEIGHSLGLFHSANTEALMYPLYhSLTDLTRFRLSQDDINGIQSLYG 264
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDpphGINLFLVAAHEIGHALGLGHSSDPGAIMYPTY-SPLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 287-477 9.48e-78

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: 241.06  E-value: 9.48e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939 287 PANCDPaLSFDAVSTLRGEILIFKDRHFWRKSLRKLEPELHLISSFWPSLPSGVDAAYEVTSKDLVFIFKGNQFWAIRGN 366
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939 367 EVRAGYPRGIHTLGFPPTVRKIDAAISDKEKNKTYFFVEDKYWRFDEKRNSMEPGFPKQIAEDFPGIDSKIDAVFEEFGF 446
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 46854939 447 FYFF-TGSSQLEFDPNAKK--VTHTLKSNS-WLNC 477
Cdd:cd00094 160 YYYFfKGDQYWRFDPRSKEvrVGYPLKISSdWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 25-87 8.74e-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: 48.67  E-value: 8.74e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46854939    25 RGEDTSmnLVQKYLEN--YYDLEKDvkqfvrrKDSGP-VVKKIREMQKFLGLEVTGKLDSDTLEVM 87
Cdd:pfam01471   1 SGEDVK--ELQRYLNRlgYYPGPVD-------GYFGPsTEAAVKAFQRAFGLPVDGIVDPETLAAL 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 1.72e-96

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: 287.59  E-value: 1.72e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939   108 KWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAP 187
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939   188 GPGINGDAHFDDDEQWTKDTT---GTNLFLVAAHEIGHSLGLFHSANTEALMYPLYhSLTDLTRFRLSQDDINGIQSLYG 264
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDpphGINLFLVAAHEIGHALGLGHSSDPGAIMYPTY-SPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 108-264 3.56e-84

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: 255.98  E-value: 3.56e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939 108 KWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRL-YEGEADIMISFAVREHGDFYPFDGPGNVLAHAYA 186
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939 187 PGpGINGDAHFDDDEQWTKDT--TGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTdlTRFRLSQDDINGIQSLYG 264
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLGSdsGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV--PKFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 287-477 9.48e-78

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: 241.06  E-value: 9.48e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939 287 PANCDPaLSFDAVSTLRGEILIFKDRHFWRKSLRKLEPELHLISSFWPSLPSGVDAAYEVTSKDLVFIFKGNQFWAIRGN 366
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939 367 EVRAGYPRGIHTLGFPPTVRKIDAAISDKEKNKTYFFVEDKYWRFDEKRNSMEPGFPKQIAEDFPGIDSKIDAVFEEFGF 446
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 46854939 447 FYFF-TGSSQLEFDPNAKK--VTHTLKSNS-WLNC 477
Cdd:cd00094 160 YYYFfKGDQYWRFDPRSKEvrVGYPLKISSdWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 105-265 8.86e-35

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: 126.70  E-value: 8.86e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939    105 GIPKWRKTHLTYRIvnYTPDLPKDAvDSAVEKALKVWEEVTPLTFSRLYeGEADIMISFAVREHGDFYpfdgpgnvlAHA 184
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVERT-GTADIYISFGSGDSGCTL---------SHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939    185 YAPGpginGDAHFDDdEQWTKDTTgtnlflVAAHEIGHSLGLFHSANTEA---LMYPLYHSlTDLTRFRLSQDDINGIQS 261
Cdd:smart00235  68 GRPG----GDQHLSL-GNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTN-IDTRNFDLSEDDSLGIPY 135


                   ....
gi 46854939    262 LYGP 265
Cdd:smart00235 136 DYGS 139
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 388-435 8.34e-12

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: 59.56  E-value: 8.34e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 46854939    388 IDAAISDKEkNKTYFFVEDKYWRFDEKRnsMEPGFPKQIAEDFPGIDS 435
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 388-433 5.53e-10

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: 54.49  E-value: 5.53e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 46854939   388 IDAAISDKEkNKTYFFVEDKYWRFDEKRnsMEPGFPKQIAeDFPGI 433
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQR--VEPGYPKLIS-DFPGL 42
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 25-87 8.74e-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: 48.67  E-value: 8.74e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46854939    25 RGEDTSmnLVQKYLEN--YYDLEKDvkqfvrrKDSGP-VVKKIREMQKFLGLEVTGKLDSDTLEVM 87
Cdd:pfam01471   1 SGEDVK--ELQRYLNRlgYYPGPVD-------GYFGPsTEAAVKAFQRAFGLPVDGIVDPETLAAL 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 1.72e-96

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: 287.59  E-value: 1.72e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939   108 KWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAP 187
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939   188 GPGINGDAHFDDDEQWTKDTT---GTNLFLVAAHEIGHSLGLFHSANTEALMYPLYhSLTDLTRFRLSQDDINGIQSLYG 264
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDpphGINLFLVAAHEIGHALGLGHSSDPGAIMYPTY-SPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 108-264 3.56e-84

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: 255.98  E-value: 3.56e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939 108 KWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRL-YEGEADIMISFAVREHGDFYPFDGPGNVLAHAYA 186
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939 187 PGpGINGDAHFDDDEQWTKDT--TGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTdlTRFRLSQDDINGIQSLYG 264
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLGSdsGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV--PKFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 287-477 9.48e-78

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: 241.06  E-value: 9.48e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939 287 PANCDPaLSFDAVSTLRGEILIFKDRHFWRKSLRKLEPELHLISSFWPSLPSGVDAAYEVTSKDLVFIFKGNQFWAIRGN 366
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939 367 EVRAGYPRGIHTLGFPPTVRKIDAAISDKEKNKTYFFVEDKYWRFDEKRNSMEPGFPKQIAEDFPGIDSKIDAVFEEFGF 446
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 46854939 447 FYFF-TGSSQLEFDPNAKK--VTHTLKSNS-WLNC 477
Cdd:cd00094 160 YYYFfKGDQYWRFDPRSKEvrVGYPLKISSdWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 105-265 8.86e-35

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: 126.70  E-value: 8.86e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939    105 GIPKWRKTHLTYRIvnYTPDLPKDAvDSAVEKALKVWEEVTPLTFSRLYeGEADIMISFAVREHGDFYpfdgpgnvlAHA 184
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVERT-GTADIYISFGSGDSGCTL---------SHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939    185 YAPGpginGDAHFDDdEQWTKDTTgtnlflVAAHEIGHSLGLFHSANTEA---LMYPLYHSlTDLTRFRLSQDDINGIQS 261
Cdd:smart00235  68 GRPG----GDQHLSL-GNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTN-IDTRNFDLSEDDSLGIPY 135


                   ....
gi 46854939    262 LYGP 265
Cdd:smart00235 136 DYGS 139
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 114-263 6.99e-16

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: 75.25  E-value: 6.99e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939 114 LTYRIVNYT----PDLPKDAVDSAVEKALKVWEEVTPLTF--SRLYEGEADIMISFAvreHGDFypfdgPGNVLAHAYAP 187
Cdd:cd00203   3 IPYVVVADDrdveEENLSAQIQSLILIAMQIWRDYLNIRFvlVGVEIDKADIAILVT---RQDF-----DGGTGGWAYLG 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939 188 G--PGINGDAHFDDDEQWTKDttgtnLFLVAAHEIGHSLGLFHSANTEA--------------------LMYPLYHSLTD 245
Cdd:cd00203  75 RvcDSLRGVGVLQDNQSGTKE-----GAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKGSFSD 149

                       170
                ....*....|....*...
gi 46854939 246 LTRFRLSQDDINGIQSLY 263
Cdd:cd00203 150 GQRKDFSQCDIDQINKLY 167
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 132-264 7.30e-15

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: 72.83  E-value: 7.30e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939 132 SAVEKALKVWEEVTPLTFSRLYEGE-ADIMISFavrehgdfypFDGP-GNVLAHAYAPGPGIN----GDAHFDDDEQWTK 205
Cdd:cd04277  37 AAARDALEAWEDVADIDFVEVSDNSgADIRFGN----------SSDPdGNTAGYAYYPGSGSGtaygGDIWFNSSYDTNS 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939 206 DTTGTNLFLVAAHEIGHSLGLFHSANTEA----------------LM-YPLYHSLTDLTRFRLSQ----DDINGIQSLYG 264
Cdd:cd04277 107 DSPGSYGYQTIIHEIGHALGLEHPGDYNGgdpvpptyaldsreytVMsYNSGYGNGASAGGGYPQtpmlLDIAALQYLYG 186
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 119-264 7.64e-15

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: 71.72  E-value: 7.64e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939 119 VNYTPDLPKDAVDS---AVEKALKVWEEVTPLTF--SRLYEGEADIMISFAVREHGDfypfdGPGNVLAHAYAPGPGING 193
Cdd:cd04279   8 IDPTPAPPDSRAQSwlqAVKQAAAEWENVGPLKFvyNPEEDNDADIVIFFDRPPPVG-----GAGGGLARAGFPLISDGN 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46854939 194 DA---HFDDDEQWTKDTTGTNLFLVAAHEIGHSLGLFH-SANTEALMYPLYHSLTDLTRfRLSQDDINGIQSLYG 264
Cdd:cd04279  83 RKlfnRTDINLGPGQPRGAENLQAIALHELGHALGLWHhSDRPEDAMYPSQGQGPDGNP-TLSARDVATLKRLYG 156
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 388-435 8.34e-12

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: 59.56  E-value: 8.34e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 46854939    388 IDAAISDKEkNKTYFFVEDKYWRFDEKRnsMEPGFPKQIAEDFPGIDS 435
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 388-433 5.53e-10

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: 54.49  E-value: 5.53e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 46854939   388 IDAAISDKEkNKTYFFVEDKYWRFDEKRnsMEPGFPKQIAeDFPGI 433
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQR--VEPGYPKLIS-DFPGL 42
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 114-263 6.09e-10

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: 57.89  E-value: 6.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939 114 LTYRIVNYTPDlpkdAVDSAVEKALKVWEEVTPLTFSRLYEG-EADIMISFaVRehgdfypfDGPGNVLAHAYAPG--PG 190
Cdd:cd04268   4 ITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNANDVdPADIRYSV-IR--------WIPYNDGTWSYGPSqvDP 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939 191 INGDAHFDDDEQWT--KDTTGTNLFLVAAHEIGHSLGLFHS----------------ANTEALMYPLYHS----LTDLTR 248
Cdd:cd04268  71 LTGEILLARVYLYSsfVEYSGARLRNTAEHELGHALGLRHNfaasdrddnvdllaekGDTSSVMDYAPSNfsiqLGDGQK 150

                       170
                ....*....|....*
gi 46854939 249 FRLSQDDINGIQSLY 263
Cdd:cd04268 151 YTIGPYDIAAIKKLY 165
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 25-87 8.74e-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: 48.67  E-value: 8.74e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46854939    25 RGEDTSmnLVQKYLEN--YYDLEKDvkqfvrrKDSGP-VVKKIREMQKFLGLEVTGKLDSDTLEVM 87
Cdd:pfam01471   1 SGEDVK--ELQRYLNRlgYYPGPVD-------GYFGPsTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 340-383 8.82e-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: 8.82e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 46854939   340 VDAAYEVtSKDLVFIFKGNQFWAIRGNEVRAGYPRGIHTL-GFPP 383
Cdd:pfam00045   1 IDAAFED-RDGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLPC 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 296-338 1.00e-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: 45.31  E-value: 1.00e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 46854939    296 FDAVSTLR-GEILIFKDRHFWRKSLRKLEP-ELHLISSFWPSLPS 338
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDPgYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 296-338 1.21e-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: 42.17  E-value: 1.21e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 46854939   296 FDAVSTLR-GEILIFKDRHFWRKSLRKLEP-ELHLISSFwPSLPS 338
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVEPgYPKLISDF-PGLPC 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 340-383 3.24e-05

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 41.07  E-value: 3.24e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 46854939    340 VDAAYEVtSKDLVFIFKGNQFWAIRGNEVRAGYPRGIHTL--GFPP 383
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFfpGLPC 45
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 178-264 1.43e-04

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: 42.79  E-value: 1.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939 178 GNVLAHAYAPGPGINGDahfddDEQWTKDTTGTNL-FLVAAHEIGHSLGLFHSANTEA----------LMYPlyhSLTDL 246
Cdd:cd04267 103 GDILGLAYVGSMCNPYS-----SVGVVEDTGFTLLtALTMAHELGHNLGAEHDGGDELafecdgggnyIMAP---VDSGL 174

                        90
                ....*....|....*...
gi 46854939 247 TRFRLSQDDINGIQSLYG 264
Cdd:cd04267 175 NSYRFSQCSIGSIREFLD 192
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 108-228 2.69e-03

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


Pssm-ID: 239819 [Multi-domain]  Cd Length: 198  Bit Score: 38.90  E-value: 2.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46854939 108 KWRKTHlTYRIVNYTPdlPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFavREHGDFYPFDGPGNVLAHayAP 187
Cdd:cd04327   2 LWRNGT-VLRIAFLGG--PDAFLKDKVRAAAREWLPYANLKFKFVTDADADIRISF--TPGDGYWSYVGTDALLIG--AD 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 46854939 188 GPGINgdahFDDDEQWTKDTTGTNlflVAAHEIGHSLGLFH 228
Cdd:cd04327  75 APTMN----LGWFTDDTPDPEFSR---VVLHEFGHALGFIH 108
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
 170-228 7.11e-03

Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma protein A (PAPP-A or pappalysin-1) cleaves insulin-like growth factor-binding proteins 4 and 5, thereby promoting cell growth by releasing bound growth factor. This model includes pappalysins and related metalloprotease domains from all three kingdoms of life. The three-dimensional structure of an archaeal representative, ulilysin, has been solved.


Pssm-ID: 239802 [Multi-domain]  Cd Length: 225  Bit Score: 38.09  E-value: 7.11e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46854939 170 DFYPFDGpGNVLAHAYAPGPGINGDAHFD----DDEQWTKDTTGT-NLFLVAAHEIGHSLGLFH 228
Cdd:cd04275  91 YVANFLG-GGLLGYATFPDSLVSLAFITDgvviNPSSLPGGSAAPyNLGDTATHEVGHWLGLYH 153
 
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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