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Conserved domains on  [gi|23308683|ref|NP_694423|]
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matrix metalloproteinase-21 isoform 1 precursor [Mus musculus]

Protein Classification

M10A family metallopeptidase( domain architecture ID 10477974)

M10A family metallopeptidase similar to matrix metalloproteinases with a C-terminal hemopexin repeat-containing domain that may be endopeptidases that degrade various components of the extracellular matrix

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 170-326 2.13e-64

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: 207.44  E-value: 2.13e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683 170 FSKKTLTWRLVGdaYSSQLSGDEQRYIFRLAFRMWSEVTPLDFREdrTAPGTMVDIKLGFGRGRHlGCPRVFDGSGQEFA 249
Cdd:cd04278   2 WSKTNLTYRILN--YPPDLPRDDVRRAIARAFRVWSDVTPLTFRE--VTSGQEADIRISFARGNH-GDGYPFDGPGGTLA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683 250 HAW----RLGEIHFDDDEHFTPLSSDTGISLLKVAVHEIGHVLGLPHTYRVGSIMQPNYIPQEPAFELDWADRKAIQRLY 325
Cdd:cd04278  77 HAFfpggIGGDIHFDDDEQWTLGSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALY 156


                .
gi 23308683 326 G 326
Cdd:cd04278 157 G 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 328-544 1.42e-28

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: 112.40  E-value: 1.42e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683 328 CKG-SFDTVFDwIRKErnqygevrvrfnTYFFRNSWYWLyenRNNRTRYGDPLQILTGWRGIPtQSIDAyvhVWSWG-KD 405
Cdd:cd00094   4 CDPlSFDAVTT-LRGE------------LYFFKGRYFWR---LSPGKPPGSPFLISSFWPSLP-SPVDA---AFERPdTG 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683 406 ERYFFKGSQYWRYDSENDQAHtedeqgrsYPKLISE-GFPGIPSPLDTAFYDRRQQLIYFFKESLVFAFDVNRNQVLNSY 484
Cdd:cd00094  64 KIYFFKGDKYWVYTGKNLEPG--------YPKPISDlGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGY 135

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683 485 PKKMSQVFPAImpqnhpfRNLDSAYYSYAHNSIFFFKGNSYWKvVSDKDKQQNTRLPLNG 544
Cdd:cd00094 136 PKLIETDFPGV-------PDKVDAAFRWLDGYYYFFKGDQYWR-FDPRSKEVRVGYPLKI 187
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 48-107 3.13e-07

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: 47.51  E-value: 3.13e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683    48 ADLHDAQSFLLKYGWSEIPSPKESagvpvGFTLAQAVRRFQKANRLPASGELDSPTLAAM 107
Cdd:pfam01471   3 EDVKELQRYLNRLGYYPGPVDGYF-----GPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 170-326 2.13e-64

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: 207.44  E-value: 2.13e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683 170 FSKKTLTWRLVGdaYSSQLSGDEQRYIFRLAFRMWSEVTPLDFREdrTAPGTMVDIKLGFGRGRHlGCPRVFDGSGQEFA 249
Cdd:cd04278   2 WSKTNLTYRILN--YPPDLPRDDVRRAIARAFRVWSDVTPLTFRE--VTSGQEADIRISFARGNH-GDGYPFDGPGGTLA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683 250 HAW----RLGEIHFDDDEHFTPLSSDTGISLLKVAVHEIGHVLGLPHTYRVGSIMQPNYIPQEPAFELDWADRKAIQRLY 325
Cdd:cd04278  77 HAFfpggIGGDIHFDDDEQWTLGSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALY 156


                .
gi 23308683 326 G 326
Cdd:cd04278 157 G 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 169-326 1.72e-62

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: 202.46  E-value: 1.72e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683   169 AFSKKTLTWRLVGdaYSSQLSGDEQRYIFRLAFRMWSEVTPLDFREDRTAPGtmvDIKLGFGRGRHlGCPRVFDGSGQEF 248
Cdd:pfam00413   1 KWRKKNLTYRILN--YTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEA---DIMIGFGRGDH-GDGYPFDGPGGVL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683   249 AHAW-----RLGEIHFDDDEHFTPLSSDT-GISLLKVAVHEIGHVLGLPHTYRVGSIMQPNYIPQEPA-FELDWADRKAI 321
Cdd:pfam00413  75 AHAFfpgpgLGGDIHFDDDETWTVGSDPPhGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKkFRLSQDDIKGI 154


                  ....*
gi 23308683   322 QRLYG 326
Cdd:pfam00413 155 QQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 328-544 1.42e-28

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: 112.40  E-value: 1.42e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683 328 CKG-SFDTVFDwIRKErnqygevrvrfnTYFFRNSWYWLyenRNNRTRYGDPLQILTGWRGIPtQSIDAyvhVWSWG-KD 405
Cdd:cd00094   4 CDPlSFDAVTT-LRGE------------LYFFKGRYFWR---LSPGKPPGSPFLISSFWPSLP-SPVDA---AFERPdTG 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683 406 ERYFFKGSQYWRYDSENDQAHtedeqgrsYPKLISE-GFPGIPSPLDTAFYDRRQQLIYFFKESLVFAFDVNRNQVLNSY 484
Cdd:cd00094  64 KIYFFKGDKYWVYTGKNLEPG--------YPKPISDlGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGY 135

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683 485 PKKMSQVFPAImpqnhpfRNLDSAYYSYAHNSIFFFKGNSYWKvVSDKDKQQNTRLPLNG 544
Cdd:cd00094 136 PKLIETDFPGV-------PDKVDAAFRWLDGYYYFFKGDQYWR-FDPRSKEVRVGYPLKI 187
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 166-327 3.60e-21

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: 89.72  E-value: 3.60e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683    166 ASRAFSKKTLTWRLVGDAYSSqlsgdEQRYIFRLAFRMWSEVTPLDFREDRTAPgtmvDIKLGFGRGRHlGCPRvfdgsg 245
Cdd:smart00235   1 GSKKWPKGTVPYVIDSSSLSP-----EEREAIAKALAEWSDVTCIRFVERTGTA----DIYISFGSGDS-GCTL------ 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683    246 qefAHAWR-LGEIHFDDDehftplssdTGISLLKVAVHEIGHVLGLPHT-YR--VGSIMQPNYIPQEP-AFELDWADRKA 320
Cdd:smart00235  65 ---SHAGRpGGDQHLSLG---------NGCINTGVAAHELGHALGLYHEqSRsdRDNYMYINYTNIDTrNFDLSEDDSLG 132


                   ....*..
gi 23308683    321 IQRLYGS 327
Cdd:smart00235 133 IPYDYGS 139
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 393-448 1.28e-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: 48.01  E-value: 1.28e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 23308683    393 IDAYVhvwSWGKDERYFFKGSQYWRYDSENDQahtedeqgRSYPKLISEGFPGIPS 448
Cdd:smart00120   1 IDAAF---ELRDGKTYFFKGDKYWRFDPKRVD--------PGYPKLISSFFPGLPC 45
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 48-107 3.13e-07

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: 47.51  E-value: 3.13e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683    48 ADLHDAQSFLLKYGWSEIPSPKESagvpvGFTLAQAVRRFQKANRLPASGELDSPTLAAM 107
Cdd:pfam01471   3 EDVKELQRYLNRLGYYPGPVDGYF-----GPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 393-448 9.08e-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: 9.08e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 23308683   393 IDAyvhVWSWGKDERYFFKGSQYWRYDSENDQahtedeqgRSYPKLISEgFPGIPS 448
Cdd:pfam00045   1 IDA---AFEDRDGKTYFFKGRKYWRFDPQRVE--------PGYPKLISD-FPGLPC 44
YcbB COG2989
Murein L,D-transpeptidase YcbB/YkuD [Cell wall/membrane/envelope biogenesis];
79-119 1.70e-04

Murein L,D-transpeptidase YcbB/YkuD [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442228 [Multi-domain]  Cd Length: 529  Bit Score: 44.55  E-value: 1.70e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 23308683  79 TLAQAVRRFQKANRLPASGELDSPTLAAMNKPrcgvPDTRL 119
Cdd:COG2989 240 ELVEAVKRFQARHGLKADGVIGPATLAALNVS----PEERI 276
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
276-292 1.91e-04

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 42.22  E-value: 1.91e-04
                         10
                 ....*....|....*..
gi 23308683  276 LLKVAVHEIGHVLGLPH 292
Cdd:NF033823 122 LAKEAVHELGHLLGLGH 138
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
276-292 2.44e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 42.25  E-value: 2.44e-04
                        10
                ....*....|....*..
gi 23308683 276 LLKVAVHEIGHVLGLPH 292
Cdd:COG1913 123 VLKEAVHELGHLFGLGH 139
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 170-326 2.13e-64

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: 207.44  E-value: 2.13e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683 170 FSKKTLTWRLVGdaYSSQLSGDEQRYIFRLAFRMWSEVTPLDFREdrTAPGTMVDIKLGFGRGRHlGCPRVFDGSGQEFA 249
Cdd:cd04278   2 WSKTNLTYRILN--YPPDLPRDDVRRAIARAFRVWSDVTPLTFRE--VTSGQEADIRISFARGNH-GDGYPFDGPGGTLA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683 250 HAW----RLGEIHFDDDEHFTPLSSDTGISLLKVAVHEIGHVLGLPHTYRVGSIMQPNYIPQEPAFELDWADRKAIQRLY 325
Cdd:cd04278  77 HAFfpggIGGDIHFDDDEQWTLGSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPKFKLSQDDIRGIQALY 156


                .
gi 23308683 326 G 326
Cdd:cd04278 157 G 157
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 169-326 1.72e-62

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: 202.46  E-value: 1.72e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683   169 AFSKKTLTWRLVGdaYSSQLSGDEQRYIFRLAFRMWSEVTPLDFREDRTAPGtmvDIKLGFGRGRHlGCPRVFDGSGQEF 248
Cdd:pfam00413   1 KWRKKNLTYRILN--YTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEA---DIMIGFGRGDH-GDGYPFDGPGGVL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683   249 AHAW-----RLGEIHFDDDEHFTPLSSDT-GISLLKVAVHEIGHVLGLPHTYRVGSIMQPNYIPQEPA-FELDWADRKAI 321
Cdd:pfam00413  75 AHAFfpgpgLGGDIHFDDDETWTVGSDPPhGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKkFRLSQDDIKGI 154


                  ....*
gi 23308683   322 QRLYG 326
Cdd:pfam00413 155 QQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 328-544 1.42e-28

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: 112.40  E-value: 1.42e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683 328 CKG-SFDTVFDwIRKErnqygevrvrfnTYFFRNSWYWLyenRNNRTRYGDPLQILTGWRGIPtQSIDAyvhVWSWG-KD 405
Cdd:cd00094   4 CDPlSFDAVTT-LRGE------------LYFFKGRYFWR---LSPGKPPGSPFLISSFWPSLP-SPVDA---AFERPdTG 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683 406 ERYFFKGSQYWRYDSENDQAHtedeqgrsYPKLISE-GFPGIPSPLDTAFYDRRQQLIYFFKESLVFAFDVNRNQVLNSY 484
Cdd:cd00094  64 KIYFFKGDKYWVYTGKNLEPG--------YPKPISDlGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGY 135

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683 485 PKKMSQVFPAImpqnhpfRNLDSAYYSYAHNSIFFFKGNSYWKvVSDKDKQQNTRLPLNG 544
Cdd:cd00094 136 PKLIETDFPGV-------PDKVDAAFRWLDGYYYFFKGDQYWR-FDPRSKEVRVGYPLKI 187
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 321-494 1.39e-21

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: 92.76  E-value: 1.39e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683 321 IQRLYGSCKGSFDTVFDWIRKERnqygevrvrfnTYFFRNSWYWLYENRNNRTRYGDPLQILtGWrGIPTQSIDAyvhVW 400
Cdd:cd00094  42 ISSFWPSLPSPVDAAFERPDTGK-----------IYFFKGDKYWVYTGKNLEPGYPKPISDL-GF-PPTVKQIDA---AL 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683 401 SWGKDER-YFFKGSQYWRYDSENDQahtedeQGRSYPKLISEGFPGIPSPLDTAFYDRRQqLIYFFKESLVFAFDVNRNQ 479
Cdd:cd00094 106 RWPDNGKtYFFKGDKYWRYDEKTQK------MDPGYPKLIETDFPGVPDKVDAAFRWLDG-YYYFFKGDQYWRFDPRSKE 178

                       170
                ....*....|....*
gi 23308683 480 VLNSYPKKMSQVFPA 494
Cdd:cd00094 179 VRVGYPLKISSDWLG 193
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 166-327 3.60e-21

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: 89.72  E-value: 3.60e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683    166 ASRAFSKKTLTWRLVGDAYSSqlsgdEQRYIFRLAFRMWSEVTPLDFREDRTAPgtmvDIKLGFGRGRHlGCPRvfdgsg 245
Cdd:smart00235   1 GSKKWPKGTVPYVIDSSSLSP-----EEREAIAKALAEWSDVTCIRFVERTGTA----DIYISFGSGDS-GCTL------ 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683    246 qefAHAWR-LGEIHFDDDehftplssdTGISLLKVAVHEIGHVLGLPHT-YR--VGSIMQPNYIPQEP-AFELDWADRKA 320
Cdd:smart00235  65 ---SHAGRpGGDQHLSLG---------NGCINTGVAAHELGHALGLYHEqSRsdRDNYMYINYTNIDTrNFDLSEDDSLG 132


                   ....*..
gi 23308683    321 IQRLYGS 327
Cdd:smart00235 133 IPYDYGS 139
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 177-326 3.66e-10

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: 59.35  E-value: 3.66e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683 177 WRLVGDAYSSQLSGDEQRYIfRLAFRMWSEVTPLDFREdrTAPGTMVDIKLGFGRGRHLGCPRVFDGSGQEFAHAWRlGE 256
Cdd:cd04277  20 GREEDTTNTAALSAAQQAAA-RDALEAWEDVADIDFVE--VSDNSGADIRFGNSSDPDGNTAGYAYYPGSGSGTAYG-GD 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683 257 IHFDD--DEHFTPLSSDTGisllKVAVHEIGHVLGL--PHTYRVG--------------SIM----QPNYIPQEPAFELD 314
Cdd:cd04277  96 IWFNSsyDTNSDSPGSYGY----QTIIHEIGHALGLehPGDYNGGdpvpptyaldsreyTVMsynsGYGNGASAGGGYPQ 171

                       170
                ....*....|....*
gi 23308683 315 W---ADRKAIQRLYG 326
Cdd:cd04277 172 TpmlLDIAALQYLYG 186
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 172-325 6.17e-10

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 58.28  E-value: 6.17e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683 172 KKTLTWRLvGDAYSSQLsgdeqRYIFRLAFRMWSEVTPLDFRE-DRTAPGtmvDIKLGFGRGRHLGC------PRVFDGS 244
Cdd:cd04268   1 KKPITYYI-DDSVPDKL-----RAAILDAIEAWNKAFAIGFKNaNDVDPA---DIRYSVIRWIPYNDgtwsygPSQVDPL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683 245 GqefahawrlGEIHFDDDEHFTPLSSDTGISLLKVAVHEIGHVLGLPH----------------TYRVGSIMQP---NYI 305
Cdd:cd04268  72 T---------GEILLARVYLYSSFVEYSGARLRNTAEHELGHALGLRHnfaasdrddnvdllaeKGDTSSVMDYapsNFS 142

                       170       180
                ....*....|....*....|...
gi 23308683 306 PQEPAFE---LDWADRKAIQRLY 325
Cdd:cd04268 143 IQLGDGQkytIGPYDIAAIKKLY 165
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 200-326 1.93e-08

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: 53.61  E-value: 1.93e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683 200 AFRMWSEVTPLDFREDrTAPGTMVDIKLGFGRGRHLG-----CPRVFDGSGQEFAhawRLGEIHFDDDehFTPLSSDTGI 274
Cdd:cd04279  29 AAAEWENVGPLKFVYN-PEEDNDADIVIFFDRPPPVGgagggLARAGFPLISDGN---RKLFNRTDIN--LGPGQPRGAE 102

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 23308683 275 SLLKVAVHEIGHVLGLPHTY-RVGSIMQPNYIPQEP-AFELDWADRKAIQRLYG 326
Cdd:cd04279 103 NLQAIALHELGHALGLWHHSdRPEDAMYPSQGQGPDgNPTLSARDVATLKRLYG 156
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 393-448 1.28e-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: 48.01  E-value: 1.28e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 23308683    393 IDAYVhvwSWGKDERYFFKGSQYWRYDSENDQahtedeqgRSYPKLISEGFPGIPS 448
Cdd:smart00120   1 IDAAF---ELRDGKTYFFKGDKYWRFDPKRVD--------PGYPKLISSFFPGLPC 45
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 48-107 3.13e-07

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: 47.51  E-value: 3.13e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683    48 ADLHDAQSFLLKYGWSEIPSPKESagvpvGFTLAQAVRRFQKANRLPASGELDSPTLAAM 107
Cdd:pfam01471   3 EDVKELQRYLNRLGYYPGPVDGYF-----GPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 173-325 4.26e-07

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: 50.21  E-value: 4.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683 173 KTLTWRLVGD--AYSSQLSGDEQRYIFRLAFRMWSEVTPLDFREDRTAPGTmVDIKLGFGRGrhlgcprvfDGSGQEFAH 250
Cdd:cd00203   1 KVIPYVVVADdrDVEEENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIDK-ADIAILVTRQ---------DFDGGTGGW 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308683 251 AW-------RLGEIHFDDDehftplsSDTGISLLKVAVHEIGHVLGLPH--------------------TYRVGSIMQP- 302
Cdd:cd00203  71 AYlgrvcdsLRGVGVLQDN-------QSGTKEGAQTIAHELGHALGFYHdhdrkdrddyptiddtlnaeDDDYYSVMSYt 143

                       170       180
                ....*....|....*....|....*.
gi 23308683 303 ---NYIPQEPAFELDwaDRKAIQRLY 325
Cdd:cd00203 144 kgsFSDGQRKDFSQC--DIDQINKLY 167
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 393-448 9.08e-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: 9.08e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 23308683   393 IDAyvhVWSWGKDERYFFKGSQYWRYDSENDQahtedeqgRSYPKLISEgFPGIPS 448
Cdd:pfam00045   1 IDA---AFEDRDGKTYFFKGRKYWRFDPQRVE--------PGYPKLISD-FPGLPC 44
YcbB COG2989
Murein L,D-transpeptidase YcbB/YkuD [Cell wall/membrane/envelope biogenesis];
79-119 1.70e-04

Murein L,D-transpeptidase YcbB/YkuD [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442228 [Multi-domain]  Cd Length: 529  Bit Score: 44.55  E-value: 1.70e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 23308683  79 TLAQAVRRFQKANRLPASGELDSPTLAAMNKPrcgvPDTRL 119
Cdd:COG2989 240 ELVEAVKRFQARHGLKADGVIGPATLAALNVS----PEERI 276
PGRP COG3409
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ...
 81-109 1.84e-04

Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442635 [Multi-domain]  Cd Length: 69  Bit Score: 39.89  E-value: 1.84e-04
                        10        20
                ....*....|....*....|....*....
gi 23308683  81 AQAVRRFQKANRLPASGELDSPTLAAMNK 109
Cdd:COG3409  41 EAAVRAFQRANGLPVDGIVGPATWAALRA 69
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
276-292 1.91e-04

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 42.22  E-value: 1.91e-04
                         10
                 ....*....|....*..
gi 23308683  276 LLKVAVHEIGHVLGLPH 292
Cdd:NF033823 122 LAKEAVHELGHLLGLGH 138
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
276-292 2.44e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 42.25  E-value: 2.44e-04
                        10
                ....*....|....*..
gi 23308683 276 LLKVAVHEIGHVLGLPH 292
Cdd:COG1913 123 VLKEAVHELGHLFGLGH 139
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 276-292 7.23e-04

Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events.


Pssm-ID: 213029  Cd Length: 173  Bit Score: 40.74  E-value: 7.23e-04
                        10
                ....*....|....*..
gi 23308683 276 LLKVAVHEIGHVLGLPH 292
Cdd:cd11375 123 LLKEAVHELGHLFGLDH 139
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 272-311 1.50e-03

Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239803  Cd Length: 197  Bit Score: 40.00  E-value: 1.50e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 23308683 272 TGISLLKVAVHEIGHVLGLPHTYRvGSIMQPNYIPQEPAF 311
Cdd:cd04276 112 LAASLRYLLAHEVGHTLGLRHNFK-ASSDGSNEELEDPLG 150
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 271-302 3.11e-03

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


Pssm-ID: 239801  Cd Length: 207  Bit Score: 39.14  E-value: 3.11e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 23308683 271 DTGISLLKVAVHEIGHVLGLPH---------TYRVGSIMQP 302
Cdd:cd04273 135 DTGLSSAFTIAHELGHVLGMPHdgdgnscgpEGKDGHIMSP 175
DUF4953 pfam16313
Met-zincin; This is a family of uncharacterized proteins that carry the highly characteriztic ...
 279-308 5.54e-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: 39.16  E-value: 5.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 23308683   279 VAVHEIGHVLGLPHTYR---------------------VGSIM---QPNYIPQE 308
Cdd:pfam16313  16 VSAHEVGHTLGLRHNFAassaypvdslrdksftrkygtTPSIMdyaRFNYVAQP 69
 
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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