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Conserved domains on  [gi|261490798|ref|NP_001159780|]
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stromelysin-1 precursor [Sus scrofa]

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 3.47e-93

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: 279.12  E-value: 3.47e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798  108 KWRKNDLTYRIVNYTLDLPRSVIDSTIEKALKIWEEVTPLTFSKISEGEADIMITFAVREHGDFSPFDGPGKVLAHAYAP 187
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798  188 GPGIYGEAHFDDDEQWTKDT---SGVNLFLVAAHELGHSLGLFHSTDSNALMYPVYNPLtDLARFRLSQDDVNGIQSLYG 264
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSdppHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPL-DSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 287-477 3.08e-73

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: 229.51  E-value: 3.08e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798 287 PATCDPaLSFDAISTLRGEILFFKDRHFWRKSFRRLEPEFHLISSFWPPLPSSIDAACEVISKDTVFIFKGTQFWAIRGN 366
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798 367 DVQPGYPRSIHTLGFPSTVKKIDAAISDKETKKTYFFVEDKYWRFDEKRQSMEPGFPKQIVEDFPGVEPKVDAVFEAFGF 446
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDG 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 261490798 447 FY-FFNGSSQFEFDPNAKK--VTHVLKSNK-WLNC 477
Cdd:cd00094  160 YYyFFKGDQYWRFDPRSKEvrVGYPLKISSdWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 34-87 6.21e-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: 49.05  E-value: 6.21e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 261490798   34 VQKYLEDYYNLTkdvkQVVRRKDSSLVVKKIQEMQKFLGLEVTGKLDSNTLEVM 87
Cdd:pfam01471   8 LQRYLNRLGYYP----GPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 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 3.47e-93

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: 279.12  E-value: 3.47e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798  108 KWRKNDLTYRIVNYTLDLPRSVIDSTIEKALKIWEEVTPLTFSKISEGEADIMITFAVREHGDFSPFDGPGKVLAHAYAP 187
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798  188 GPGIYGEAHFDDDEQWTKDT---SGVNLFLVAAHELGHSLGLFHSTDSNALMYPVYNPLtDLARFRLSQDDVNGIQSLYG 264
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSdppHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPL-DSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 108-264 1.21e-78

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: 241.72  E-value: 1.21e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798 108 KWRKNDLTYRIVNYTLDLPRSVIDSTIEKALKIWEEVTPLTFSKI-SEGEADIMITFAVREHGDFSPFDGPGKVLAHAYA 186
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798 187 PGpGIYGEAHFDDDEQWTKDT--SGVNLFLVAAHELGHSLGLFHSTDSNALMYPVYNPLTDlaRFRLSQDDVNGIQSLYG 264
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTLGSdsGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP--KFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 287-477 3.08e-73

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: 229.51  E-value: 3.08e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798 287 PATCDPaLSFDAISTLRGEILFFKDRHFWRKSFRRLEPEFHLISSFWPPLPSSIDAACEVISKDTVFIFKGTQFWAIRGN 366
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798 367 DVQPGYPRSIHTLGFPSTVKKIDAAISDKETKKTYFFVEDKYWRFDEKRQSMEPGFPKQIVEDFPGVEPKVDAVFEAFGF 446
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDG 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 261490798 447 FY-FFNGSSQFEFDPNAKK--VTHVLKSNK-WLNC 477
Cdd:cd00094  160 YYyFFKGDQYWRFDPRSKEvrVGYPLKISSdWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 105-264 8.24e-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: 8.24e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798   105 GLPKWRKNDLTYRIVNYTLDlprSVIDSTIEKALKIWEEVTPLTFSKISeGEADIMITFAVREHGDFspfdgpgkvLAHA 184
Cdd:smart00235   1 GSKKWPKGTVPYVIDSSSLS---PEEREAIAKALAEWSDVTCIRFVERT-GTADIYISFGSGDSGCT---------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798   185 YAPGpgiyGEAHFDDdEQWTKDTSgvnlflVAAHELGHSLGLFHSTDSNA---LMYPVYNPlTDLARFRLSQDDVNGIQS 261
Cdd:smart00235  68 GRPG----GDQHLSL-GNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTN-IDTRNFDLSEDDSLGIPY 135


                   ...
gi 261490798   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 1.85e-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: 56.10  E-value: 1.85e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 261490798   388 IDAAISDKETKkTYFFVEDKYWRFDEKRqsMEPGFPKQIVEDFPGVEP 435
Cdd:smart00120   1 IDAAFELRDGK-TYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 388-435 1.88e-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: 50.26  E-value: 1.88e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 261490798  388 IDAAISDKEtKKTYFFVEDKYWRFDEKRqsMEPGFPKQIvEDFPGVEP 435
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQR--VEPGYPKLI-SDFPGLPC 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 34-87 6.21e-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: 49.05  E-value: 6.21e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 261490798   34 VQKYLEDYYNLTkdvkQVVRRKDSSLVVKKIQEMQKFLGLEVTGKLDSNTLEVM 87
Cdd:pfam01471   8 LQRYLNRLGYYP----GPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
185-238 4.40e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 38.01  E-value: 4.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798 185 YAPG-PGIYGEAHFDD----------DEQWTKDTSGVNLFL-----VAAHELGHSLGLFHSTDSNALMYP 238
Cdd:COG1913   80 YAPGlNFVFGLAYLGGrvavvstarlRPEFYGLPPDEELFLervlkEAVHELGHLFGLGHCPNPRCVMHF 149
 
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 3.47e-93

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: 279.12  E-value: 3.47e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798  108 KWRKNDLTYRIVNYTLDLPRSVIDSTIEKALKIWEEVTPLTFSKISEGEADIMITFAVREHGDFSPFDGPGKVLAHAYAP 187
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798  188 GPGIYGEAHFDDDEQWTKDT---SGVNLFLVAAHELGHSLGLFHSTDSNALMYPVYNPLtDLARFRLSQDDVNGIQSLYG 264
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSdppHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPL-DSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 108-264 1.21e-78

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: 241.72  E-value: 1.21e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798 108 KWRKNDLTYRIVNYTLDLPRSVIDSTIEKALKIWEEVTPLTFSKI-SEGEADIMITFAVREHGDFSPFDGPGKVLAHAYA 186
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798 187 PGpGIYGEAHFDDDEQWTKDT--SGVNLFLVAAHELGHSLGLFHSTDSNALMYPVYNPLTDlaRFRLSQDDVNGIQSLYG 264
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTLGSdsGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP--KFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 287-477 3.08e-73

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: 229.51  E-value: 3.08e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798 287 PATCDPaLSFDAISTLRGEILFFKDRHFWRKSFRRLEPEFHLISSFWPPLPSSIDAACEVISKDTVFIFKGTQFWAIRGN 366
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798 367 DVQPGYPRSIHTLGFPSTVKKIDAAISDKETKKTYFFVEDKYWRFDEKRQSMEPGFPKQIVEDFPGVEPKVDAVFEAFGF 446
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLDG 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 261490798 447 FY-FFNGSSQFEFDPNAKK--VTHVLKSNK-WLNC 477
Cdd:cd00094  160 YYyFFKGDQYWRFDPRSKEvrVGYPLKISSdWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 105-264 8.24e-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: 8.24e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798   105 GLPKWRKNDLTYRIVNYTLDlprSVIDSTIEKALKIWEEVTPLTFSKISeGEADIMITFAVREHGDFspfdgpgkvLAHA 184
Cdd:smart00235   1 GSKKWPKGTVPYVIDSSSLS---PEEREAIAKALAEWSDVTCIRFVERT-GTADIYISFGSGDSGCT---------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798   185 YAPGpgiyGEAHFDDdEQWTKDTSgvnlflVAAHELGHSLGLFHSTDSNA---LMYPVYNPlTDLARFRLSQDDVNGIQS 261
Cdd:smart00235  68 GRPG----GDQHLSL-GNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTN-IDTRNFDLSEDDSLGIPY 135


                   ...
gi 261490798   262 LYG 264
Cdd:smart00235 136 DYG 138
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 114-263 5.66e-18

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: 81.03  E-value: 5.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798 114 LTYRIVNYT----LDLPRSVIDSTIEKALKIWEEVTPLTF--SKISEGEADIMITFAvreHGDFspfdgPGKVLAHAYAP 187
Cdd:cd00203    3 IPYVVVADDrdveEENLSAQIQSLILIAMQIWRDYLNIRFvlVGVEIDKADIAILVT---RQDF-----DGGTGGWAYLG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798 188 G--PGIYGEAHFDDDEQWTKDtsgvnLFLVAAHELGHSLGLFHSTDSNA--------------------LMYPVYNPLTD 245
Cdd:cd00203   75 RvcDSLRGVGVLQDNQSGTKE-----GAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKGSFSD 149

                        170
                 ....*....|....*...
gi 261490798 246 LARFRLSQDDVNGIQSLY 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 ...
 132-264 1.08e-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: 1.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798 132 STIEKALKIWEEVTPLTFSKISEGE--ADIMITFAVREHGDFSpfDGPGKVLAHAYAPGPGIYGEAHFDDDEQWTKDTSG 209
Cdd:cd04279   24 QAVKQAAAEWENVGPLKFVYNPEEDndADIVIFFDRPPPVGGA--GGGLARAGFPLISDGNRKLFNRTDINLGPGQPRGA 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 261490798 210 VNLFLVAAHELGHSLGLFHSTD-SNALMYPVYNPLTDLARfRLSQDDVNGIQSLYG 264
Cdd:cd04279  102 ENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNP-TLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 132-264 3.88e-14

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: 70.52  E-value: 3.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798 132 STIEKALKIWEEVTPLTFSKISEGE-ADIMItfavrehGDFSPFDGPgkVLAHAYAPGPGIY----GEAHFDDDEQWTKD 206
Cdd:cd04277   37 AAARDALEAWEDVADIDFVEVSDNSgADIRF-------GNSSDPDGN--TAGYAYYPGSGSGtaygGDIWFNSSYDTNSD 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261490798 207 TSGVNLFLVAAHELGHSLGLFHSTDSNA----------------LM-Y--PVYNPLTDLARF--RLSQDDVNGIQSLYG 264
Cdd:cd04277  108 SPGSYGYQTIIHEIGHALGLEHPGDYNGgdpvpptyaldsreytVMsYnsGYGNGASAGGGYpqTPMLLDIAALQYLYG 186
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 388-435 1.85e-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: 56.10  E-value: 1.85e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 261490798   388 IDAAISDKETKkTYFFVEDKYWRFDEKRqsMEPGFPKQIVEDFPGVEP 435
Cdd:smart00120   1 IDAAFELRDGK-TYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGLPC 45
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 111-263 4.74e-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: 58.28  E-value: 4.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798 111 KNDLTYRIVNYTLDlprsVIDSTIEKALKIWEEVTPLTFSKISEG-EADIMITFavreHGDFSPFDGpgkvlAHAYAPGP 189
Cdd:cd04268    1 KKPITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNANDVdPADIRYSV----IRWIPYNDG-----TWSYGPSQ 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798 190 GIY--GEAHFDDDEQWT--KDTSGVNLFLVAAHELGHSLGLFHS----------------TDSNALMYPVYN----PLTD 245
Cdd:cd04268   68 VDPltGEILLARVYLYSsfVEYSGARLRNTAEHELGHALGLRHNfaasdrddnvdllaekGDTSSVMDYAPSnfsiQLGD 147

                        170
                 ....*....|....*...
gi 261490798 246 LARFRLSQDDVNGIQSLY 263
Cdd:cd04268  148 GQKYTIGPYDIAAIKKLY 165
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 388-435 1.88e-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: 50.26  E-value: 1.88e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 261490798  388 IDAAISDKEtKKTYFFVEDKYWRFDEKRqsMEPGFPKQIvEDFPGVEP 435
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQR--VEPGYPKLI-SDFPGLPC 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 34-87 6.21e-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: 49.05  E-value: 6.21e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 261490798   34 VQKYLEDYYNLTkdvkQVVRRKDSSLVVKKIQEMQKFLGLEVTGKLDSNTLEVM 87
Cdd:pfam01471   8 LQRYLNRLGYYP----GPVDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 340-383 2.35e-07

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: 47.18  E-value: 2.35e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 261490798  340 IDAACEvISKDTVFIFKGTQFWAIRGNDVQPGYPRSIHTL-GFPS 383
Cdd:pfam00045   1 IDAAFE-DRDGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLPC 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 296-338 2.42e-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: 47.24  E-value: 2.42e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 261490798   296 FDAISTLR-GEILFFKDRHFWRKSFRRLEPEF-HLISSFWPPLPS 338
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDPGYpKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 296-333 8.11e-06

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: 42.55  E-value: 8.11e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 261490798  296 FDAISTLR-GEILFFKDRHFWRKSFRRLEPEF-HLISSFW 333
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVEPGYpKLISDFP 40
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 340-383 1.57e-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: 41.84  E-value: 1.57e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 261490798   340 IDAACEvISKDTVFIFKGTQFWAIRGNDVQPGYPRSIHTL--GFPS 383
Cdd:smart00120   1 IDAAFE-LRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFfpGLPC 45
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 178-264 1.94e-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: 42.41  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798 178 GKVLAHAYAPGPG-IYGEAHFDDDEQWTKDTSgvnlfLVAAHELGHSLGLFHSTDS----------NALMYPVynpLTDL 246
Cdd:cd04267  103 GDILGLAYVGSMCnPYSSVGVVEDTGFTLLTA-----LTMAHELGHNLGAEHDGGDelafecdgggNYIMAPV---DSGL 174

                         90
                 ....*....|....*...
gi 261490798 247 ARFRLSQDDVNGIQSLYG 264
Cdd:cd04267  175 NSYRFSQCSIGSIREFLD 192
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
185-238 4.40e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 38.01  E-value: 4.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261490798 185 YAPG-PGIYGEAHFDD----------DEQWTKDTSGVNLFL-----VAAHELGHSLGLFHSTDSNALMYP 238
Cdd:COG1913   80 YAPGlNFVFGLAYLGGrvavvstarlRPEFYGLPPDEELFLervlkEAVHELGHLFGLGHCPNPRCVMHF 149
 
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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