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Conserved domains on  [gi|1935598140|ref|NP_598198|]
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stromelysin-2 precursor [Rattus norvegicus]

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 1.01e-92

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: 277.96  E-value: 1.01e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140 108 KWRKNHISYRIVNYTLDLPRESVDSAIERALKVWEEVTPLTFSRISEGEADIMISFAVGEHGDFYPFDGVGQSLAHAYPP 187
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140 188 GPGFYGDAHFDDDEKWSLG---PSGTNLFLVAAHELGHSLGLFHSNNKESLMYPVYRFsTSQANIRLSQDDIEGIQSLYG 264
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGsdpPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSP-LDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 286-476 1.41e-83

Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat.


:

Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 256.08  E-value: 1.41e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140 286 PVKCDPaLSFDAVTMLRGEFLFFKDRHFWRRTQWNPEPEFHLISAFWPSLPSGLDAAYEANNKDRVLIFKGSQFWAVRGN 365
Cdd:cd00094     1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140 366 EVQAGYPKRIHTLGFPPTVKKIDAAVFEKEKKKTYFFVGDKYWRFDETRQLMDKGFPRLITDDFPGIEPQVDAVLHAF-G 444
Cdd:cd00094    80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLdG 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1935598140 445 FFYFFRGSSQFEFDPNART--VTHTLKSNS-WLLC 476
Cdd:cd00094   160 YYYFFKGDQYWRFDPRSKEvrVGYPLKISSdWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 33-87 6.60e-06

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


:

Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 43.27  E-value: 6.60e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1935598140  33 LAQQYLEKYYNFRKNEKQFFkrkdSSPVVKKIEEMQKFLGLEMTGKLDSNTVEMM 87
Cdd:pfam01471   7 ELQRYLNRLGYYPGPVDGYF----GPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 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 1.01e-92

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: 277.96  E-value: 1.01e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140 108 KWRKNHISYRIVNYTLDLPRESVDSAIERALKVWEEVTPLTFSRISEGEADIMISFAVGEHGDFYPFDGVGQSLAHAYPP 187
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140 188 GPGFYGDAHFDDDEKWSLG---PSGTNLFLVAAHELGHSLGLFHSNNKESLMYPVYRFsTSQANIRLSQDDIEGIQSLYG 264
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGsdpPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSP-LDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 286-476 1.41e-83

Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat.


Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 256.08  E-value: 1.41e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140 286 PVKCDPaLSFDAVTMLRGEFLFFKDRHFWRRTQWNPEPEFHLISAFWPSLPSGLDAAYEANNKDRVLIFKGSQFWAVRGN 365
Cdd:cd00094     1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140 366 EVQAGYPKRIHTLGFPPTVKKIDAAVFEKEKKKTYFFVGDKYWRFDETRQLMDKGFPRLITDDFPGIEPQVDAVLHAF-G 444
Cdd:cd00094    80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLdG 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1935598140 445 FFYFFRGSSQFEFDPNART--VTHTLKSNS-WLLC 476
Cdd:cd00094   160 YYYFFKGDQYWRFDPRSKEvrVGYPLKISSdWLGC 194
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 108-264 7.59e-81

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


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 247.50  E-value: 7.59e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140 108 KWRKNHISYRIVNYTLDLPRESVDSAIERALKVWEEVTPLTFSRI-SEGEADIMISFAVGEHGDFYPFDGVGQSLAHAYP 186
Cdd:cd04278     1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140 187 PGpGFYGDAHFDDDEKWSLG--PSGTNLFLVAAHELGHSLGLFHSNNKESLMYPVYRFSTSqaNIRLSQDDIEGIQSLYG 264
Cdd:cd04278    81 PG-GIGGDIHFDDDEQWTLGsdSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP--KFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 105-265 1.25e-34

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: 126.31  E-value: 1.25e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140  105 GSPKWRKNHISYRIVNYTLDlprESVDSAIERALKVWEEVTPLTFSRISeGEADIMISFAVGEHGDFYpfdgvgqslAHA 184
Cdd:smart00235   1 GSKKWPKGTVPYVIDSSSLS---PEEREAIAKALAEWSDVTCIRFVERT-GTADIYISFGSGDSGCTL---------SHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140  185 YPPGpgfyGDAHFDDdEKWSLGpsgtnlFLVAAHELGHSLGLFHSNNK---ESLMYPVYRFSTSQaNIRLSQDDIEGIQS 261
Cdd:smart00235  68 GRPG----GDQHLSL-GNGCIN------TGVAAHELGHALGLYHEQSRsdrDNYMYINYTNIDTR-NFDLSEDDSLGIPY 135


                   ....
gi 1935598140  262 LYGA 265
Cdd:smart00235 136 DYGS 139
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 387-434 2.31e-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: 61.49  E-value: 2.31e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1935598140  387 IDAAvFEKEKKKTYFFVGDKYWRFDETRqlMDKGFPRLITDDFPGIEP 434
Cdd:smart00120   1 IDAA-FELRDGKTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 387-434 2.48e-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: 55.65  E-value: 2.48e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1935598140 387 IDAAvFEKEKKKTYFFVGDKYWRFDETRqlMDKGFPRLITdDFPGIEP 434
Cdd:pfam00045   1 IDAA-FEDRDGKTYFFKGRKYWRFDPQR--VEPGYPKLIS-DFPGLPC 44
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 205-263 1.36e-07

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 52.38  E-value: 1.36e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1935598140 205 LGPSGTNLFLVAA--HELGHSLGLF-HSNNKESLMYpvyrFSTSQANIRLSQDDIEGIQSLY 263
Cdd:COG5549   173 LSPNQTGKYLLATarHELGHALGIWgHSPSPTDAMY----FSQVRNPPPISPRDINTLKRIY 230
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 33-87 6.60e-06

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 43.27  E-value: 6.60e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1935598140  33 LAQQYLEKYYNFRKNEKQFFkrkdSSPVVKKIEEMQKFLGLEMTGKLDSNTVEMM 87
Cdd:pfam01471   7 ELQRYLNRLGYYPGPVDGYF----GPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
metzin_BF0631 TIGR03952
zinc-dependent metalloproteinase lipoprotein, BF0631 family; Members of this protein family ...
 198-228 2.22e-03

zinc-dependent metalloproteinase lipoprotein, BF0631 family; Members of this protein family are zinc-dependent metalloproteinases, related to ulilysin and other members of the pappalysin family. Members occur as predicted lipoproteins and occur mostly in the genera Bacteriodes and Prevotella. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 274876  Cd Length: 351  Bit Score: 40.15  E-value: 2.22e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1935598140 198 DDDEKWSLGPSGTNLFLVAAHELGHSLGLFH 228
Cdd:TIGR03952 218 DDPNKKGYIYSSADFNVTLAHELGHYLGLFH 248
 
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 1.01e-92

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: 277.96  E-value: 1.01e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140 108 KWRKNHISYRIVNYTLDLPRESVDSAIERALKVWEEVTPLTFSRISEGEADIMISFAVGEHGDFYPFDGVGQSLAHAYPP 187
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140 188 GPGFYGDAHFDDDEKWSLG---PSGTNLFLVAAHELGHSLGLFHSNNKESLMYPVYRFsTSQANIRLSQDDIEGIQSLYG 264
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGsdpPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSP-LDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 286-476 1.41e-83

Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat.


Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 256.08  E-value: 1.41e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140 286 PVKCDPaLSFDAVTMLRGEFLFFKDRHFWRRTQWNPEPEFHLISAFWPSLPSGLDAAYEANNKDRVLIFKGSQFWAVRGN 365
Cdd:cd00094     1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140 366 EVQAGYPKRIHTLGFPPTVKKIDAAVFEKEKKKTYFFVGDKYWRFDETRQLMDKGFPRLITDDFPGIEPQVDAVLHAF-G 444
Cdd:cd00094    80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWLdG 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1935598140 445 FFYFFRGSSQFEFDPNART--VTHTLKSNS-WLLC 476
Cdd:cd00094   160 YYYFFKGDQYWRFDPRSKEvrVGYPLKISSdWLGC 194
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 108-264 7.59e-81

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


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 247.50  E-value: 7.59e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140 108 KWRKNHISYRIVNYTLDLPRESVDSAIERALKVWEEVTPLTFSRI-SEGEADIMISFAVGEHGDFYPFDGVGQSLAHAYP 186
Cdd:cd04278     1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140 187 PGpGFYGDAHFDDDEKWSLG--PSGTNLFLVAAHELGHSLGLFHSNNKESLMYPVYRFSTSqaNIRLSQDDIEGIQSLYG 264
Cdd:cd04278    81 PG-GIGGDIHFDDDEQWTLGsdSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP--KFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 105-265 1.25e-34

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: 126.31  E-value: 1.25e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140  105 GSPKWRKNHISYRIVNYTLDlprESVDSAIERALKVWEEVTPLTFSRISeGEADIMISFAVGEHGDFYpfdgvgqslAHA 184
Cdd:smart00235   1 GSKKWPKGTVPYVIDSSSLS---PEEREAIAKALAEWSDVTCIRFVERT-GTADIYISFGSGDSGCTL---------SHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140  185 YPPGpgfyGDAHFDDdEKWSLGpsgtnlFLVAAHELGHSLGLFHSNNK---ESLMYPVYRFSTSQaNIRLSQDDIEGIQS 261
Cdd:smart00235  68 GRPG----GDQHLSL-GNGCIN------TGVAAHELGHALGLYHEQSRsdrDNYMYINYTNIDTR-NFDLSEDDSLGIPY 135


                   ....
gi 1935598140  262 LYGA 265
Cdd:smart00235 136 DYGS 139
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 132-264 1.06e-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: 75.14  E-value: 1.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140 132 SAIERALKVWEEVTPLTFSRISEGE-ADIMISFAVGEHGDFYpfdgvgqslAHAYPPGPGFY----GDAHFDDDEKWSLG 206
Cdd:cd04277    37 AAARDALEAWEDVADIDFVEVSDNSgADIRFGNSSDPDGNTA---------GYAYYPGSGSGtaygGDIWFNSSYDTNSD 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1935598140 207 PSGTNLFLVAAHELGHSLGLFHSNNK------------ESLMYPV--YRFSTS-------QANIRLSQDDIEGIQSLYG 264
Cdd:cd04277   108 SPGSYGYQTIIHEIGHALGLEHPGDYnggdpvpptyalDSREYTVmsYNSGYGngasaggGYPQTPMLLDIAALQYLYG 186
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 129-264 4.48e-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: 72.49  E-value: 4.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140 129 SVDSAIERALKVWEEVTPLTFSRISEGE--ADIMISFavgehGDFYPFDGVGQSLA-HAYPPGPGFYGDA--HFDDDEKW 203
Cdd:cd04279    21 SWLQAVKQAAAEWENVGPLKFVYNPEEDndADIVIFF-----DRPPPVGGAGGGLArAGFPLISDGNRKLfnRTDINLGP 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1935598140 204 SLGPSGTNLFLVAAHELGHSLGLFH-SNNKESLMYPVYRfSTSQANIRLSQDDIEGIQSLYG 264
Cdd:cd04279    96 GQPRGAENLQAIALHELGHALGLWHhSDRPEDAMYPSQG-QGPDGNPTLSARDVATLKRLYG 156
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 114-263 6.04e-13

Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 66.78  E-value: 6.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140 114 ISYRIVNYT----LDLPRESVDSAIERALKVWEEVTPLTF--SRISEGEADIMISFAVGEHGdfypfdgvGQSLAHAYPP 187
Cdd:cd00203     3 IPYVVVADDrdveEENLSAQIQSLILIAMQIWRDYLNIRFvlVGVEIDKADIAILVTRQDFD--------GGTGGWAYLG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140 188 G--PGFYGDAHFDDDEKWslgpsGTNLFLVAAHELGHSLGLFHSNNKE--------------------SLMYPVYRFSTS 245
Cdd:cd00203    75 RvcDSLRGVGVLQDNQSG-----TKEGAQTIAHELGHALGFYHDHDRKdrddyptiddtlnaedddyySVMSYTKGSFSD 149

                         170
                  ....*....|....*...
gi 1935598140 246 QANIRLSQDDIEGIQSLY 263
Cdd:cd00203   150 GQRKDFSQCDIDQINKLY 167
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 387-434 2.31e-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: 61.49  E-value: 2.31e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1935598140  387 IDAAvFEKEKKKTYFFVGDKYWRFDETRqlMDKGFPRLITDDFPGIEP 434
Cdd:smart00120   1 IDAA-FELRDGKTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 387-434 2.48e-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: 55.65  E-value: 2.48e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1935598140 387 IDAAvFEKEKKKTYFFVGDKYWRFDETRqlMDKGFPRLITdDFPGIEP 434
Cdd:pfam00045   1 IDAA-FEDRDGKTYFFKGRKYWRFDPQR--VEPGYPKLIS-DFPGLPC 44
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 118-263 2.55e-08

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: 53.27  E-value: 2.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140 118 IVNYTLDLPRESVDSAIERALKVWEEVTPLTFS-RISEGEADIMISFAVGEHGDfypfdgvgqSLAHAYppGPGFY---- 192
Cdd:cd04268     4 ITYYIDDSVPDKLRAAILDAIEAWNKAFAIGFKnANDVDPADIRYSVIRWIPYN---------DGTWSY--GPSQVdplt 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140 193 GDAHFDDDEKWS--LGPSGTNLFLVAAHELGHSLGLFHSNN----------------KESLMYPVYRFSTSQANIR---- 250
Cdd:cd04268    73 GEILLARVYLYSsfVEYSGARLRNTAEHELGHALGLRHNFAasdrddnvdllaekgdTSSVMDYAPSNFSIQLGDGqkyt 152

                         170
                  ....*....|...
gi 1935598140 251 LSQDDIEGIQSLY 263
Cdd:cd04268   153 IGPYDIAAIKKLY 165
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 205-263 1.36e-07

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 52.38  E-value: 1.36e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1935598140 205 LGPSGTNLFLVAA--HELGHSLGLF-HSNNKESLMYpvyrFSTSQANIRLSQDDIEGIQSLY 263
Cdd:COG5549   173 LSPNQTGKYLLATarHELGHALGIWgHSPSPTDAMY----FSQVRNPPPISPRDINTLKRIY 230
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 295-337 7.38e-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: 45.70  E-value: 7.38e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1935598140  295 FDAVTMLR-GEFLFFKDRHFWRRTQWNPEPEF-HLISAFWPSLPS 337
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDPGYpKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 339-382 8.72e-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: 45.64  E-value: 8.72e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1935598140 339 LDAAYEANNKdRVLIFKGSQFWAVRGNEVQAGYPKRIHTL-GFPP 382
Cdd:pfam00045   1 IDAAFEDRDG-KTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLPC 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 33-87 6.60e-06

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 43.27  E-value: 6.60e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1935598140  33 LAQQYLEKYYNFRKNEKQFFkrkdSSPVVKKIEEMQKFLGLEMTGKLDSNTVEMM 87
Cdd:pfam01471   7 ELQRYLNRLGYYPGPVDGYF----GPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 295-337 1.02e-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: 42.55  E-value: 1.02e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1935598140 295 FDAVTMLR-GEFLFFKDRHFWRRTQWNPEPEF-HLISAFwPSLPS 337
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVEPGYpKLISDF-PGLPC 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 339-382 4.09e-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: 40.69  E-value: 4.09e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1935598140  339 LDAAYEANNkDRVLIFKGSQFWAVRGNEVQAGYPKRIHTL--GFPP 382
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDPKRVDPGYPKLISSFfpGLPC 45
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
 108-228 6.43e-04

Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family contain two conserved disulphide bridges, these are joined 1-4 and 2-3. Members of this family have an amino terminal propeptide which is cleaved to give the active protease domain. All other linked domains are found to the carboxyl terminus of this domain. This family includes: Astacin, a digestive enzyme from Crayfish. Meprin, a multiple domain membrane component that is constructed from a homologous alpha and beta chain. Proteins involved in morphogenesis such as Swiss:P13497, and Tolloid from drosophila.


Pssm-ID: 426242 [Multi-domain]  Cd Length: 192  Bit Score: 40.73  E-value: 6.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1935598140 108 KWRKNHISYRIVNYTLDLPResvdSAIERALKVWEEVTPLTFSRiSEGEADIMISFavgehgdFYPFDGVGQSLAHAYPP 187
Cdd:pfam01400   2 KWPNGPIPYVIDGSLTGLAR----ALIRQAMRHWENKTCIRFVE-RTPAPDNNYLF-------FFKGDGCYSYVGRVGGR 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1935598140 188 GPgfygdahfdddekWSLGPsGTNLFLVAAHELGHSLGLFH 228
Cdd:pfam01400  70 QP-------------VSIGD-GCDKFGIIVHELGHALGFFH 96
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
215-245 1.82e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 39.17  E-value: 1.82e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1935598140 215 VAAHELGHSLGLFHSNNKESLMYpvyrFSTS 245
Cdd:COG1913   126 EAVHELGHLFGLGHCPNPRCVMH----FSNS 152
metzin_BF0631 TIGR03952
zinc-dependent metalloproteinase lipoprotein, BF0631 family; Members of this protein family ...
 198-228 2.22e-03

zinc-dependent metalloproteinase lipoprotein, BF0631 family; Members of this protein family are zinc-dependent metalloproteinases, related to ulilysin and other members of the pappalysin family. Members occur as predicted lipoproteins and occur mostly in the genera Bacteriodes and Prevotella. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 274876  Cd Length: 351  Bit Score: 40.15  E-value: 2.22e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1935598140 198 DDDEKWSLGPSGTNLFLVAAHELGHSLGLFH 228
Cdd:TIGR03952 218 DDPNKKGYIYSSADFNVTLAHELGHYLGLFH 248
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 203-229 3.41e-03

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 37.35  E-value: 3.41e-03
                          10        20
                  ....*....|....*....|....*..
gi 1935598140 203 WSLGPSGTNLFLVAAHELGHSLGLFHS 229
Cdd:pfam13582  96 SGSGPVGDTGADTFAHEIGHNFGLNHT 122
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 210-244 5.64e-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: 37.98  E-value: 5.64e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1935598140 210 TNLFLVA---AHELGHSLGLFHSNNK-----------ESLMYPVYRFST 244
Cdd:cd04269   126 RNLLLFAvtmAHELGHNLGMEHDDGGctcgrstcimaPSPSSLTDAFSN 174
DUF4953 pfam16313
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ...
 215-239 7.56e-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: 7.56e-03
                          10        20
                  ....*....|....*....|....*
gi 1935598140 215 VAAHELGHSLGLFHsNNKESLMYPV 239
Cdd:pfam16313  16 VSAHEVGHTLGLRH-NFAASSAYPV 39
 
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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