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Conserved domains on  [gi|73808268|ref|NP_071405|]
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matrix metalloproteinase-27 precursor [Homo sapiens]

Protein Classification

matrix metalloproteinase( domain architecture ID 12021147)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 106-261 5.65e-89

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: 269.49  E-value: 5.65e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808268   106 WRKYNLTYRIINYTPDMARAAVDEAIQEGLEVWSKVTPLKFTKISKGIADIMIAFRTRVHGRcPRYFDGPLGVLGHAFPP 185
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGD-GYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73808268   186 GPGLGGDTHFDEDENWTKDGA---GFNLFLVAAHEFGHALGLSHSNDQTALMFPNYVSLDPRKYPLSQDDINGIQSIYG 261
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDpphGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 276-465 1.05e-64

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: 208.32  E-value: 1.05e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808268 276 PHACDPdLTFDAITTFRREVMFFKGRHLWRIYYDITDVEFELIASFWPSLPADLQAAYENP-RDKILVFKDENFWMIRGY 354
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPdTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808268 355 AVLPDYPKSIHTLGFPGRVKKIDAAVCDKTTRKTYFFVGIWCWRFDEMTQTMDKGFPQRVVKHFPGISIRVDAAFQY-KG 433
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWlDG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 73808268 434 FFFFSRGSKQFEYDIKTK--NITRIMRTNT-WFQC 465
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSKevRVGYPLKISSdWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 26-86 4.54e-10

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: 55.21  E-value: 4.54e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 73808268    26 NEENMQLAQAYLNQFYSLEIEgnhlVQSKNRSLIDDKIREMQAFFGLTVTGKLDSNTLEIM 86
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYPGP----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 ...
 106-261 5.65e-89

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: 269.49  E-value: 5.65e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808268   106 WRKYNLTYRIINYTPDMARAAVDEAIQEGLEVWSKVTPLKFTKISKGIADIMIAFRTRVHGRcPRYFDGPLGVLGHAFPP 185
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGD-GYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73808268   186 GPGLGGDTHFDEDENWTKDGA---GFNLFLVAAHEFGHALGLSHSNDQTALMFPNYVSLDPRKYPLSQDDINGIQSIYG 261
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDpphGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 106-261 7.72e-69

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: 217.84  E-value: 7.72e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808268 106 WRKYNLTYRIINYTPDMARAAVDEAIQEGLEVWSKVTPLKFTKISKGI-ADIMIAFRTRVHGrCPRYFDGPLGVLGHAFP 184
Cdd:cd04278   2 WSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISFARGNHG-DGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73808268 185 PGpGLGGDTHFDEDENWTKDGA--GFNLFLVAAHEFGHALGLSHSNDQTALMFPNYVSLDPrKYPLSQDDINGIQSIYG 261
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLGSDsgGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 276-465 1.05e-64

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: 208.32  E-value: 1.05e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808268 276 PHACDPdLTFDAITTFRREVMFFKGRHLWRIYYDITDVEFELIASFWPSLPADLQAAYENP-RDKILVFKDENFWMIRGY 354
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPdTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808268 355 AVLPDYPKSIHTLGFPGRVKKIDAAVCDKTTRKTYFFVGIWCWRFDEMTQTMDKGFPQRVVKHFPGISIRVDAAFQY-KG 433
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWlDG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 73808268 434 FFFFSRGSKQFEYDIKTK--NITRIMRTNT-WFQC 465
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSKevRVGYPLKISSdWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 106-261 6.76e-29

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: 111.29  E-value: 6.76e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808268    106 WRKYNLTYRIinYTPDMARAAvDEAIQEGLEVWSKVTPLKFTKISKGiADIMIAFRTRVHGRCpryfdgplgvLGHAFPP 185
Cdd:smart00235   5 WPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDSGCT----------LSHAGRP 70

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73808268    186 GpglgGDTHFDeDENWTkDGAGfnlflVAAHEFGHALGLSHS---NDQTALMFPNYVSLDPRKYPLSQDDINGIQSIYG 261
Cdd:smart00235  71 G----GDQHLS-LGNGC-INTG-----VAAHELGHALGLYHEqsrSDRDNYMYINYTNIDTRNFDLSEDDSLGIPYDYG 138
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 26-86 4.54e-10

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: 55.21  E-value: 4.54e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 73808268    26 NEENMQLAQAYLNQFYSLEIEgnhlVQSKNRSLIDDKIREMQAFFGLTVTGKLDSNTLEIM 86
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYPGP----VDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 124-260 1.70e-08

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 55.08  E-value: 1.70e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808268 124 RAAVDEAIQEglevWSKVTPLKFTKiSKGIADIMIAFRTRvhgrcpryfdgPLGvlghaFPPGPGLGG-----DTHFDED 198
Cdd:COG5549 103 VAAVLQAIAE----WNAYLPLEVVE-NPENADIIIVRSNP-----------PLT-----ASPNPETGArsaetTYEFYDT 161

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 73808268 199 EN--------WTKDGAGFNLFLVAA-HEFGHALGL-SHSNDQTALMFPNYVSLDPrkyPLSQDDINGIQSIY 260
Cdd:COG5549 162 GNilshrftiLLSPNQTGKYLLATArHELGHALGIwGHSPSPTDAMYFSQVRNPP---PISPRDINTLKRIY 230
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 376-421 3.79e-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: 43.77  E-value: 3.79e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 73808268    376 IDAAVCDKTTrKTYFFVGIWCWRFDEmtQTMDKGFPQRVVKHFPGI 421
Cdd:smart00120   1 IDAAFELRDG-KTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGL 43
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 329-370 5.93e-05

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 40.24  E-value: 5.93e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 73808268   329 LQAAYENPRDKILVFKDENFWMIRGYAVLPDYPKSIHTL-GFP 370
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLP 43
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 106-261 5.65e-89

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: 269.49  E-value: 5.65e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808268   106 WRKYNLTYRIINYTPDMARAAVDEAIQEGLEVWSKVTPLKFTKISKGIADIMIAFRTRVHGRcPRYFDGPLGVLGHAFPP 185
Cdd:pfam00413   2 WRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGD-GYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73808268   186 GPGLGGDTHFDEDENWTKDGA---GFNLFLVAAHEFGHALGLSHSNDQTALMFPNYVSLDPRKYPLSQDDINGIQSIYG 261
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDpphGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 106-261 7.72e-69

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: 217.84  E-value: 7.72e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808268 106 WRKYNLTYRIINYTPDMARAAVDEAIQEGLEVWSKVTPLKFTKISKGI-ADIMIAFRTRVHGrCPRYFDGPLGVLGHAFP 184
Cdd:cd04278   2 WSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISFARGNHG-DGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73808268 185 PGpGLGGDTHFDEDENWTKDGA--GFNLFLVAAHEFGHALGLSHSNDQTALMFPNYVSLDPrKYPLSQDDINGIQSIYG 261
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLGSDsgGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 276-465 1.05e-64

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: 208.32  E-value: 1.05e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808268 276 PHACDPdLTFDAITTFRREVMFFKGRHLWRIYYDITDVEFELIASFWPSLPADLQAAYENP-RDKILVFKDENFWMIRGY 354
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPdTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808268 355 AVLPDYPKSIHTLGFPGRVKKIDAAVCDKTTRKTYFFVGIWCWRFDEMTQTMDKGFPQRVVKHFPGISIRVDAAFQY-KG 433
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRWlDG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 73808268 434 FFFFSRGSKQFEYDIKTK--NITRIMRTNT-WFQC 465
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSKevRVGYPLKISSdWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 106-261 6.76e-29

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: 111.29  E-value: 6.76e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808268    106 WRKYNLTYRIinYTPDMARAAvDEAIQEGLEVWSKVTPLKFTKISKGiADIMIAFRTRVHGRCpryfdgplgvLGHAFPP 185
Cdd:smart00235   5 WPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDSGCT----------LSHAGRP 70

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73808268    186 GpglgGDTHFDeDENWTkDGAGfnlflVAAHEFGHALGLSHS---NDQTALMFPNYVSLDPRKYPLSQDDINGIQSIYG 261
Cdd:smart00235  71 G----GDQHLS-LGNGC-INTG-----VAAHELGHALGLYHEqsrSDRDNYMYINYTNIDTRNFDLSEDDSLGIPYDYG 138
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 130-261 2.25e-16

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: 76.34  E-value: 2.25e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808268 130 AIQEGLEVWSKVTPLKFTKI--SKGIADIMIAFRTRVH-----GRCPRYFDGPLGVLGHAFPPgpglggdtHFDEDENWT 202
Cdd:cd04279  25 AVKQAAAEWENVGPLKFVYNpeEDNDADIVIFFDRPPPvggagGGLARAGFPLISDGNRKLFN--------RTDINLGPG 96

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808268 203 KDGAGFNLFLVAAHEFGHALGLSHSNDQ-TALMFPNYVSLDPRKYPLSQDDINGIQSIYG 261
Cdd:cd04279  97 QPRGAENLQAIALHELGHALGLWHHSDRpEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 129-261 6.92e-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: 70.14  E-value: 6.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808268 129 EAIQEGLEVWSKVTPLKFTKISKG-IADIMIAFrtrvhgrcprYFDGPLGVLGHAFPPGPG----LGGDTHFDEDENWTK 203
Cdd:cd04277  37 AAARDALEAWEDVADIDFVEVSDNsGADIRFGN----------SSDPDGNTAGYAYYPGSGsgtaYGGDIWFNSSYDTNS 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808268 204 DGAGFNLFLVAAHEFGHALGLSHSND----------------QTALM----FPNYVSLDPRKYP--LSQDDINGIQSIYG 261
Cdd:cd04277 107 DSPGSYGYQTIIHEIGHALGLEHPGDynggdpvpptyaldsrEYTVMsynsGYGNGASAGGGYPqtPMLLDIAALQYLYG 186
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 121-260 2.67e-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: 67.93  E-value: 2.67e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808268 121 DMARAAVDEAIQEGLEVWSKVTPLKFTKISKGI--ADIMIaFRTRVhgrcpryfDGPLGVLGHAFPPG--PGLGGDTHFD 196
Cdd:cd00203  17 ENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIdkADIAI-LVTRQ--------DFDGGTGGWAYLGRvcDSLRGVGVLQ 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808268 197 EDENWTKDGAGfnlflVAAHEFGHALGLSHSNDQTA--------------------LMFPNYVS-LDPRKYPLSQDDING 255
Cdd:cd00203  88 DNQSGTKEGAQ-----TIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKGSfSDGQRKDFSQCDIDQ 162


                ....*
gi 73808268 256 IQSIY 260
Cdd:cd00203 163 INKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 108-260 1.10e-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: 60.20  E-value: 1.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808268 108 KYNLTYRIINYTPDMARAAVDEAIQEglevWSKVTPLKFTKISKGI-ADIMIAFrtrvhGRCPRYFDGPLGVLGHAFPPg 186
Cdd:cd04268   1 KKPITYYIDDSVPDKLRAAILDAIEA----WNKAFAIGFKNANDVDpADIRYSV-----IRWIPYNDGTWSYGPSQVDP- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808268 187 pgLGGDTHFDeDENWTKDGAGFN---LFLVAAHEFGHALGLSHSN----------------DQTALMFPNYVSL-----D 242
Cdd:cd04268  71 --LTGEILLA-RVYLYSSFVEYSgarLRNTAEHELGHALGLRHNFaasdrddnvdllaekgDTSSVMDYAPSNFsiqlgD 147

                       170
                ....*....|....*...
gi 73808268 243 PRKYPLSQDDINGIQSIY 260
Cdd:cd04268 148 GQKYTIGPYDIAAIKKLY 165
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 26-86 4.54e-10

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: 55.21  E-value: 4.54e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 73808268    26 NEENMQLAQAYLNQFYSLEIEgnhlVQSKNRSLIDDKIREMQAFFGLTVTGKLDSNTLEIM 86
Cdd:pfam01471   1 SGEDVKELQRYLNRLGYYPGP----VDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 124-260 1.70e-08

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 55.08  E-value: 1.70e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808268 124 RAAVDEAIQEglevWSKVTPLKFTKiSKGIADIMIAFRTRvhgrcpryfdgPLGvlghaFPPGPGLGG-----DTHFDED 198
Cdd:COG5549 103 VAAVLQAIAE----WNAYLPLEVVE-NPENADIIIVRSNP-----------PLT-----ASPNPETGArsaetTYEFYDT 161

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 73808268 199 EN--------WTKDGAGFNLFLVAA-HEFGHALGL-SHSNDQTALMFPNYVSLDPrkyPLSQDDINGIQSIY 260
Cdd:COG5549 162 GNilshrftiLLSPNQTGKYLLATArHELGHALGIwGHSPSPTDAMYFSQVRNPP---PISPRDINTLKRIY 230
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 376-421 3.79e-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: 43.77  E-value: 3.79e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 73808268    376 IDAAVCDKTTrKTYFFVGIWCWRFDEmtQTMDKGFPQRVVKHFPGI 421
Cdd:smart00120   1 IDAAFELRDG-KTYFFKGDKYWRFDP--KRVDPGYPKLISSFFPGL 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 329-371 5.87e-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: 40.30  E-value: 5.87e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 73808268    329 LQAAYENPRDKILVFKDENFWMIRGYAVLPDYPKSIHTLgFPG 371
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSF-FPG 42
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 329-370 5.93e-05

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 40.24  E-value: 5.93e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 73808268   329 LQAAYENPRDKILVFKDENFWMIRGYAVLPDYPKSIHTL-GFP 370
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 285-326 2.52e-04

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: 38.76  E-value: 2.52e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 73808268    285 FDAITTFRR-EVMFFKGRHLWRIYYDITDVEF-ELIASFWPSLP 326
Cdd:smart00120   1 IDAAFELRDgKTYFFKGDKYWRFDPKRVDPGYpKLISSFFPGLP 44
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 177-261 2.94e-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: 42.02  E-value: 2.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808268 177 GVLGHAFPPGPG-LGGDTHFDEDENWTKDGAgfnlfLVAAHEFGHALGLSH--------SNDQTALMFPNYVSLDPRKYP 247
Cdd:cd04267 104 DILGLAYVGSMCnPYSSVGVVEDTGFTLLTA-----LTMAHELGHNLGAEHdggdelafECDGGGNYIMAPVDSGLNSYR 178

                        90
                ....*....|....
gi 73808268 248 LSQDDINGIQSIYG 261
Cdd:cd04267 179 FSQCSIGSIREFLD 192
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 376-421 6.16e-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: 6.16e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 73808268   376 IDAAVCDKTtRKTYFFVGIWCWRFDEmtQTMDKGFPQRvVKHFPGI 421
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDP--QRVEPGYPKL-ISDFPGL 42
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 125-226 3.58e-03

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


Pssm-ID: 239819 [Multi-domain]  Cd Length: 198  Bit Score: 38.90  E-value: 3.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73808268 125 AAVDEAIQEGLEVWSKVTPLKFTKISKGIADIMIAFRTRvhgrcpryfDGPLGVLG---HAFP---PGPGLGGDTHFDED 198
Cdd:cd04327  19 AFLKDKVRAAAREWLPYANLKFKFVTDADADIRISFTPG---------DGYWSYVGtdaLLIGadaPTMNLGWFTDDTPD 89

                        90       100
                ....*....|....*....|....*...
gi 73808268 199 ENWTKdgagfnlflVAAHEFGHALGLSH 226
Cdd:cd04327  90 PEFSR---------VVLHEFGHALGFIH 108
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
213-239 6.24e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 37.63  E-value: 6.24e-03
                        10        20
                ....*....|....*....|....*...
gi 73808268 213 VAAHEFGHALGLSHSNDQTALM-FPNYV 239
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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