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Conserved domains on  [gi|894216250|ref|NP_001297646|]
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matrix metalloproteinase-27 [Mus musculus]

Protein Classification

matrix metalloproteinase( domain architecture ID 12021147)

matrix metalloproteinase is an M10A family metallopeptidase with a C-terminal hemopexin repeat-containing domain, such as stromelysin-1 (matrix metalloproteinase-3), which can degrade fibronectin, laminin, type I, III, IV, and V gelatins, collagens III, IV, X, and IX, as well as cartilage proteoglycans

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 120-276 8.24e-88

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: 267.18  E-value: 8.24e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250  120 WRKYSLTYRIMNYTPDMTPADVDEAIQKALQVWSKVTPLTFTRISKGVADIMIAFRTGVHG-WCPrhFDGPLGVLGHAFP 198
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGdGYP--FDGPGGVLAHAFF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250  199 PGLGLGGDTHFDEDETWIAKDG--EGFNLFLVAAHEFGHSLGLSHSNDQTALMFPNYISLDPSKYPLSQDDIDGIQSIYG 276
Cdd:pfam00413  80 PGPGLGGDIHFDDDETWTVGSDppHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 291-480 6.49e-67

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: 214.48  E-value: 6.49e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250 291 PHACDPtLTFDAITTFRREVMFFKGRHLWRVYSDIAGAEFEFIDSFWPSLPADLQAAYESP-RDELLVFKDENFWVIRGY 369
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPdTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250 370 SVLPGYPKSIHTLGFPRRVKKIDAAVCDHDTRKTFFFVGIWCWRYDEMAQAMDRGFPQRIIKCFPGIRLRVDAVFQ-HNG 448
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLDG 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 894216250 449 FLYFFHGSRQFEYDMKAK--NITQVIKTNS-WFLC 480
Cdd:cd00094  160 YYYFFKGDQYWRFDPRSKevRVGYPLKISSdWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 45-100 6.15e-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: 6.15e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 894216250   45 QLAQAYLNQFYSLEIEgshfVQSKNRSLFDGKLREMQAFFGLTVTGKLDSDTLAIM 100
Cdd:pfam01471   6 KELQRYLNRLGYYPGP----VDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 120-276 8.24e-88

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: 267.18  E-value: 8.24e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250  120 WRKYSLTYRIMNYTPDMTPADVDEAIQKALQVWSKVTPLTFTRISKGVADIMIAFRTGVHG-WCPrhFDGPLGVLGHAFP 198
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGdGYP--FDGPGGVLAHAFF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250  199 PGLGLGGDTHFDEDETWIAKDG--EGFNLFLVAAHEFGHSLGLSHSNDQTALMFPNYISLDPSKYPLSQDDIDGIQSIYG 276
Cdd:pfam00413  80 PGPGLGGDIHFDDDETWTVGSDppHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 120-276 1.75e-72

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: 227.47  E-value: 1.75e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250 120 WRKYSLTYRIMNYTPDMTPADVDEAIQKALQVWSKVTPLTFTRI-SKGVADIMIAFRTGVHGwCPRHFDGPLGVLGHAFP 198
Cdd:cd04278    2 WSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHG-DGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 894216250 199 PGlGLGGDTHFDEDETWIA-KDGEGFNLFLVAAHEFGHSLGLSHSNDQTALMFPNYISLDPsKYPLSQDDIDGIQSIYG 276
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTLgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 291-480 6.49e-67

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: 214.48  E-value: 6.49e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250 291 PHACDPtLTFDAITTFRREVMFFKGRHLWRVYSDIAGAEFEFIDSFWPSLPADLQAAYESP-RDELLVFKDENFWVIRGY 369
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPdTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250 370 SVLPGYPKSIHTLGFPRRVKKIDAAVCDHDTRKTFFFVGIWCWRYDEMAQAMDRGFPQRIIKCFPGIRLRVDAVFQ-HNG 448
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLDG 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 894216250 449 FLYFFHGSRQFEYDMKAK--NITQVIKTNS-WFLC 480
Cdd:cd00094  160 YYYFFKGDQYWRFDPRSKevRVGYPLKISSdWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 120-277 5.81e-31

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: 117.07  E-value: 5.81e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250   120 WRKYSLTYRImnYTPDMTPaDVDEAIQKALQVWSKVTPLTFTRISKGvADIMIAFRTGVHGwcprhfdgplGVLGHAFPP 199
Cdd:smart00235   5 WPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDSG----------CTLSHAGRP 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250   200 GlglgGDTHFDeDETWIAKDGegfnlflVAAHEFGHSLGLSHS---NDQTALMFPNYISLDPSKYPLSQDDIDGIQSIYG 276
Cdd:smart00235  71 G----GDQHLS-LGNGCINTG-------VAAHELGHALGLYHEqsrSDRDNYMYINYTNIDTRNFDLSEDDSLGIPYDYG 138


                   .
gi 894216250   277 S 277
Cdd:smart00235 139 S 139
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 45-100 6.15e-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: 6.15e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 894216250   45 QLAQAYLNQFYSLEIEgshfVQSKNRSLFDGKLREMQAFFGLTVTGKLDSDTLAIM 100
Cdd:pfam01471   6 KELQRYLNRLGYYPGP----VDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 344-385 8.81e-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: 8.81e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 894216250  344 LQAAYESPRDELLVFKDENFWVIRGYSVLPGYPKSIHTL-GFP 385
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 391-436 4.91e-06

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 43.39  E-value: 4.91e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 894216250   391 IDAAVCDHDTrKTFFFVGIWCWRYDEmaQAMDRGFPQRIIKCFPGI 436
Cdd:smart00120   1 IDAAFELRDG-KTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGL 43
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
228-254 5.43e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 38.01  E-value: 5.43e-03
                         10        20
                 ....*....|....*....|....*...
gi 894216250 228 VAAHEFGHSLGLSHSNDQTALM-FPNYI 254
Cdd:COG1913  126 EAVHELGHLFGLGHCPNPRCVMhFSNSL 153
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 120-276 8.24e-88

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: 267.18  E-value: 8.24e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250  120 WRKYSLTYRIMNYTPDMTPADVDEAIQKALQVWSKVTPLTFTRISKGVADIMIAFRTGVHG-WCPrhFDGPLGVLGHAFP 198
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGdGYP--FDGPGGVLAHAFF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250  199 PGLGLGGDTHFDEDETWIAKDG--EGFNLFLVAAHEFGHSLGLSHSNDQTALMFPNYISLDPSKYPLSQDDIDGIQSIYG 276
Cdd:pfam00413  80 PGPGLGGDIHFDDDETWTVGSDppHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 120-276 1.75e-72

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: 227.47  E-value: 1.75e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250 120 WRKYSLTYRIMNYTPDMTPADVDEAIQKALQVWSKVTPLTFTRI-SKGVADIMIAFRTGVHGwCPRHFDGPLGVLGHAFP 198
Cdd:cd04278    2 WSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHG-DGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 894216250 199 PGlGLGGDTHFDEDETWIA-KDGEGFNLFLVAAHEFGHSLGLSHSNDQTALMFPNYISLDPsKYPLSQDDIDGIQSIYG 276
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTLgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 291-480 6.49e-67

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: 214.48  E-value: 6.49e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250 291 PHACDPtLTFDAITTFRREVMFFKGRHLWRVYSDIAGAEFEFIDSFWPSLPADLQAAYESP-RDELLVFKDENFWVIRGY 369
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPdTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250 370 SVLPGYPKSIHTLGFPRRVKKIDAAVCDHDTRKTFFFVGIWCWRYDEMAQAMDRGFPQRIIKCFPGIRLRVDAVFQ-HNG 448
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLDG 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 894216250 449 FLYFFHGSRQFEYDMKAK--NITQVIKTNS-WFLC 480
Cdd:cd00094  160 YYYFFKGDQYWRFDPRSKevRVGYPLKISSdWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 120-277 5.81e-31

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: 117.07  E-value: 5.81e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250   120 WRKYSLTYRImnYTPDMTPaDVDEAIQKALQVWSKVTPLTFTRISKGvADIMIAFRTGVHGwcprhfdgplGVLGHAFPP 199
Cdd:smart00235   5 WPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDSG----------CTLSHAGRP 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250   200 GlglgGDTHFDeDETWIAKDGegfnlflVAAHEFGHSLGLSHS---NDQTALMFPNYISLDPSKYPLSQDDIDGIQSIYG 276
Cdd:smart00235  71 G----GDQHLS-LGNGCINTG-------VAAHELGHALGLYHEqsrSDRDNYMYINYTNIDTRNFDLSEDDSLGIPYDYG 138


                   .
gi 894216250   277 S 277
Cdd:smart00235 139 S 139
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 144-276 5.45e-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: 5.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250 144 AIQKALQVWSKVTPLTFTRI--SKGVADIMIAFRTgvhgwcPRHFDGPLGVLGHAFPPGLGLGGDTHFDEDETWIAKD-- 219
Cdd:cd04279   25 AVKQAAAEWENVGPLKFVYNpeEDNDADIVIFFDR------PPPVGGAGGGLARAGFPLISDGNRKLFNRTDINLGPGqp 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 894216250 220 GEGFNLFLVAAHEFGHSLGLSHSNDQ-TALMFPNYISLDPSKYPLSQDDIDGIQSIYG 276
Cdd:cd04279   99 RGAENLQAIALHELGHALGLWHHSDRpEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 143-276 3.69e-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: 70.91  E-value: 3.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250 143 EAIQKALQVWSKVTPLTFTRISKG-VADIMIAFRTGVHGwcprhfdgplGVLGHAFPPG----LGLGGDTHFDEDETWIA 217
Cdd:cd04277   37 AAARDALEAWEDVADIDFVEVSDNsGADIRFGNSSDPDG----------NTAGYAYYPGsgsgTAYGGDIWFNSSYDTNS 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250 218 KDGEGFNlFLVAAHEFGHSLGLSHSND----------------QTALM----FPNYISLDPSKYP--LSQDDIDGIQSIY 275
Cdd:cd04277  107 DSPGSYG-YQTIIHEIGHALGLEHPGDynggdpvpptyaldsrEYTVMsynsGYGNGASAGGGYPqtPMLLDIAALQYLY 185


                 .
gi 894216250 276 G 276
Cdd:cd04277  186 G 186
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 135-275 1.43e-12

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: 65.62  E-value: 1.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250 135 DMTPADVDEAIQKALQVWSKVTPLTFTRISKGV--ADIMIaFRTGVhgwcprhfDGPLGVLGHAFPPG--LGLGGDTHFD 210
Cdd:cd00203   17 ENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIdkADIAI-LVTRQ--------DFDGGTGGWAYLGRvcDSLRGVGVLQ 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250 211 EDETWiakdgeGFNLFLVAAHEFGHSLGLSHSNDQTA--------------------LMFPNYIS-LDPSKYPLSQDDID 269
Cdd:cd00203   88 DNQSG------TKEGAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKGSfSDGQRKDFSQCDID 161


                 ....*.
gi 894216250 270 GIQSIY 275
Cdd:cd00203  162 QINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 122-275 4.51e-11

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: 61.36  E-value: 4.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250 122 KYSLTYRIMNYTPDmtpaDVDEAIQKALQVWSKVTPLTFT-RISKGVADIMIafrtGVHGWCPRHfDGPLGVLGHAFPPG 200
Cdd:cd04268    1 KKPITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKnANDVDPADIRY----SVIRWIPYN-DGTWSYGPSQVDPL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250 201 LG--LGGDTHFDEDETWIAKDgegfNLFLVAAHEFGHSLGLSHSN----------------DQTALMFPNYISL-----D 257
Cdd:cd04268   72 TGeiLLARVYLYSSFVEYSGA----RLRNTAEHELGHALGLRHNFaasdrddnvdllaekgDTSSVMDYAPSNFsiqlgD 147

                        170
                 ....*....|....*...
gi 894216250 258 PSKYPLSQDDIDGIQSIY 275
Cdd:cd04268  148 GQKYTIGPYDIAAIKKLY 165
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 45-100 6.15e-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: 6.15e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 894216250   45 QLAQAYLNQFYSLEIEgshfVQSKNRSLFDGKLREMQAFFGLTVTGKLDSDTLAIM 100
Cdd:pfam01471   6 KELQRYLNRLGYYPGP----VDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 344-385 8.81e-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: 8.81e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 894216250  344 LQAAYESPRDELLVFKDENFWVIRGYSVLPGYPKSIHTL-GFP 385
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 391-436 4.91e-06

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 43.39  E-value: 4.91e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 894216250   391 IDAAVCDHDTrKTFFFVGIWCWRYDEmaQAMDRGFPQRIIKCFPGI 436
Cdd:smart00120   1 IDAAFELRDG-KTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGL 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 344-386 5.74e-06

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 43.39  E-value: 5.74e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 894216250   344 LQAAYESPRDELLVFKDENFWVIRGYSVLPGYPKSIHTL--GFPR 386
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFfpGLPC 45
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 137-241 1.25e-04

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: 43.14  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250 137 TPADVDEAIQKALQVWSKVTPLTFTRISKGVADIMIAFRTGVHGWcprhfdGPLGVLGHAFP---PGLGLGGDTHFDEDE 213
Cdd:cd04327   17 PDAFLKDKVRAAAREWLPYANLKFKFVTDADADIRISFTPGDGYW------SYVGTDALLIGadaPTMNLGWFTDDTPDP 90

                         90       100
                 ....*....|....*....|....*...
gi 894216250 214 TWIAkdgegfnlflVAAHEFGHSLGLSH 241
Cdd:cd04327   91 EFSR----------VVLHEFGHALGFIH 108
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 391-436 5.94e-04

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: 37.55  E-value: 5.94e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 894216250  391 IDAAVCDHDtRKTFFFVGIWCWRYDEmaQAMDRGFPQRIIKcFPGI 436
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDP--QRVEPGYPKLISD-FPGL 42
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 300-341 1.98e-03

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 36.07  E-value: 1.98e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 894216250   300 FDAITTFRR-EVMFFKGRHLWRVYSDIAGAEF-EFIDSFWPSLP 341
Cdd:smart00120   1 IDAAFELRDgKTYFFKGDKYWRFDPKRVDPGYpKLISSFFPGLP 44
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 128-242 2.77e-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: 37.73  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216250  128 RIMNYTPDMTP---ADVDEAIQKALQVWSkvtpltfTRISKGVADIMIAFRTgvhgwcprhfDGPLGVLGHAFPPGL--- 201
Cdd:pfam13582  26 AIIITTSADTPytsSDALEILDELQEVND-------TRIGQYGYDLGHLFTG----------RDGGGGGGIAYVGGVcns 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 894216250  202 ----GLGGDTHfdedetwiakdGEGFNLFLVAAHEFGHSLGLSHS 242
Cdd:pfam13582  89 gskfGVNSGSG-----------PVGDTGADTFAHEIGHNFGLNHT 122
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
228-254 5.43e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 38.01  E-value: 5.43e-03
                         10        20
                 ....*....|....*....|....*...
gi 894216250 228 VAAHEFGHSLGLSHSNDQTALM-FPNYI 254
Cdd:COG1913  126 EAVHELGHLFGLGHCPNPRCVMhFSNSL 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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