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Conserved domains on  [gi|4505209|ref|NP_002418|]
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collagenase 3 preproprotein [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 ...
 112-267 1.64e-95

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: 284.89  E-value: 1.64e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505209    112 KWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNFTRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPP 191
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505209    192 GPNYGGDAHFDDDETWT---SSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYG 267
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTvgsDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 281-471 2.86e-79

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: 244.91  E-value: 2.86e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505209  281 PDKCDPsLSLDAITSLRGETMIFKDRFFWRLHPQQVDAELFLTKSFWPELPNRIDAAYEHPSHDLIFIFRGRKFWALNGY 360
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505209  361 DILEGYPKKISELGLPKEVKKISAAVHFEDTGKTLLFSGNQVWRYDDTNHIMDKDYPRLIEEDFPGIGDKVDAVYE-KNG 439
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 4505209  440 YIYFFNGPIQFEYSIWS--NRIVRVMPANS-ILWC 471
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSkeVRVGYPLKISSdWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 32-91 4.35e-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: 49.44  E-value: 4.35e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4505209     32 SEEDLQFAERYLRSY-YHPTNLAGILkenaASSMTERLREMQSFFGLEVTGKLDDNTLDVM 91
Cdd:pfam01471   1 SGEDVKELQRYLNRLgYYPGPVDGYF----GPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 112-267 1.64e-95

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: 284.89  E-value: 1.64e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505209    112 KWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNFTRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPP 191
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505209    192 GPNYGGDAHFDDDETWT---SSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYG 267
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTvgsDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 112-267 5.43e-81

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


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 247.89  E-value: 5.43e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505209  112 KWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNFTRLHDGI-ADIMISFGIKEHGDFYPFDGPSGLLAHAFP 190
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505209  191 PGPnYGGDAHFDDDETWT--SSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTgKSHFMLPDDDVQGIQSLYG 267
Cdd:cd04278  81 PGG-IGGDIHFDDDEQWTlgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGP-VPKFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 281-471 2.86e-79

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: 244.91  E-value: 2.86e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505209  281 PDKCDPsLSLDAITSLRGETMIFKDRFFWRLHPQQVDAELFLTKSFWPELPNRIDAAYEHPSHDLIFIFRGRKFWALNGY 360
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505209  361 DILEGYPKKISELGLPKEVKKISAAVHFEDTGKTLLFSGNQVWRYDDTNHIMDKDYPRLIEEDFPGIGDKVDAVYE-KNG 439
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 4505209  440 YIYFFNGPIQFEYSIWS--NRIVRVMPANS-ILWC 471
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSkeVRVGYPLKISSdWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 111-268 2.45e-32

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: 120.15  E-value: 2.45e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505209     111 LKWSKMNLTYRIvnYTPDMTHSEVEkAFKKAFKVWSDVTPLNFTRLHDGiADIMISFGIKEHGDFYpfdgpsgllAHAFP 190
Cdd:smart00235   3 KKWPKGTVPYVI--DSSSLSPEERE-AIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDSGCTL---------SHAGR 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505209     191 PGpnygGDAHFDDdETWTSSSKgynlflVAAHEFGHSLGLDHSKDPGA---LMFPIYTYTGKSHFMLPDDDVQGIQSLYG 267
Cdd:smart00235  70 PG----GDQHLSL-GNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYDYG 138


                   .
gi 4505209     268 P 268
Cdd:smart00235 139 S 139
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 382-428 5.77e-09

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: 51.47  E-value: 5.77e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 4505209     382 ISAAVHFEDtGKTLLFSGNQVWRYDDTNhiMDKDYPRLIEEDFPGIG 428
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGLP 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 32-91 4.35e-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: 49.44  E-value: 4.35e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4505209     32 SEEDLQFAERYLRSY-YHPTNLAGILkenaASSMTERLREMQSFFGLEVTGKLDDNTLDVM 91
Cdd:pfam01471   1 SGEDVKELQRYLNRLgYYPGPVDGYF----GPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 334-376 2.48e-07

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 47.18  E-value: 2.48e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 4505209    334 IDAAYEHPsHDLIFIFRGRKFWALNGYDILEGYPKKISEL-GLP 376
Cdd:pfam00045   1 IDAAFEDR-DGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLP 43
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
219-242 3.80e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 38.40  E-value: 3.80e-03
                        10        20
                ....*....|....*....|....
gi 4505209  219 VAAHEFGHSLGLDHSKDPGALMFP 242
Cdd:COG1913 126 EAVHELGHLFGLGHCPNPRCVMHF 149
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 112-267 1.64e-95

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: 284.89  E-value: 1.64e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505209    112 KWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNFTRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPP 191
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505209    192 GPNYGGDAHFDDDETWT---SSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYG 267
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTvgsDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 112-267 5.43e-81

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


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 247.89  E-value: 5.43e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505209  112 KWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNFTRLHDGI-ADIMISFGIKEHGDFYPFDGPSGLLAHAFP 190
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQeADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505209  191 PGPnYGGDAHFDDDETWT--SSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTgKSHFMLPDDDVQGIQSLYG 267
Cdd:cd04278  81 PGG-IGGDIHFDDDEQWTlgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGP-VPKFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 281-471 2.86e-79

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: 244.91  E-value: 2.86e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505209  281 PDKCDPsLSLDAITSLRGETMIFKDRFFWRLHPQQVDAELFLTKSFWPELPNRIDAAYEHPSHDLIFIFRGRKFWALNGY 360
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505209  361 DILEGYPKKISELGLPKEVKKISAAVHFEDTGKTLLFSGNQVWRYDDTNHIMDKDYPRLIEEDFPGIGDKVDAVYE-KNG 439
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 4505209  440 YIYFFNGPIQFEYSIWS--NRIVRVMPANS-ILWC 471
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSkeVRVGYPLKISSdWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 111-268 2.45e-32

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: 120.15  E-value: 2.45e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505209     111 LKWSKMNLTYRIvnYTPDMTHSEVEkAFKKAFKVWSDVTPLNFTRLHDGiADIMISFGIKEHGDFYpfdgpsgllAHAFP 190
Cdd:smart00235   3 KKWPKGTVPYVI--DSSSLSPEERE-AIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDSGCTL---------SHAGR 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505209     191 PGpnygGDAHFDDdETWTSSSKgynlflVAAHEFGHSLGLDHSKDPGA---LMFPIYTYTGKSHFMLPDDDVQGIQSLYG 267
Cdd:smart00235  70 PG----GDQHLSL-GNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYDYG 138


                   .
gi 4505209     268 P 268
Cdd:smart00235 139 S 139
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 120-267 3.46e-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: 3.46e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505209  120 YRIVNYTPDMTHSEVEKAF-KKAFKVWSDVTPLNFTRLHDG-IADIMIsfgikehGDFYPFDGPSGllAHAFPPGPN--- 194
Cdd:cd04277  20 GREEDTTNTAALSAAQQAAaRDALEAWEDVADIDFVEVSDNsGADIRF-------GNSSDPDGNTA--GYAYYPGSGsgt 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505209  195 -YGGDAHFDDDETWTSSSKG-YNlFLVAAHEFGHSLGLDHSKDPGA----------------LM---FPIYTYTGKSH-- 251
Cdd:cd04277  91 aYGGDIWFNSSYDTNSDSPGsYG-YQTIIHEIGHALGLEHPGDYNGgdpvpptyaldsreytVMsynSGYGNGASAGGgy 169

                       170
                ....*....|....*....
gi 4505209  252 ---FMLpdDDVQGIQSLYG 267
Cdd:cd04277 170 pqtPML--LDIAALQYLYG 186
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 131-267 5.10e-13

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: 66.71  E-value: 5.10e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505209  131 HSEVEKAFKKAFKVWSDVTPLNF--TRLHDGIADIMISFGikehgDFYPFDGPSGLLAHAFPPGPNYGGDA---HFDDDE 205
Cdd:cd04279  19 AQSWLQAVKQAAAEWENVGPLKFvyNPEEDNDADIVIFFD-----RPPPVGGAGGGLARAGFPLISDGNRKlfnRTDINL 93

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4505209  206 TWTSSSKGYNLFLVAAHEFGHSLGLDHSKD-PGALMFPIYTYTGKSHFMLPDDDVQGIQSLYG 267
Cdd:cd04279  94 GPGQPRGAENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 118-266 4.29e-10

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: 58.30  E-value: 4.29e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505209  118 LTYRIVNYTPDM----THSEVEKAFKKAFKVWSDVTPLNFtRLHDGI---ADIMISFgikehgdfYPFDGPSGLLAHAFP 190
Cdd:cd00203   3 IPYVVVADDRDVeeenLSAQIQSLILIAMQIWRDYLNIRF-VLVGVEidkADIAILV--------TRQDFDGGTGGWAYL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505209  191 PG--PNYGGDAHFDDDETWTssskgYNLFLVAAHEFGHSLGLDHS--------------------KDPGALMFPIYT-YT 247
Cdd:cd00203  74 GRvcDSLRGVGVLQDNQSGT-----KEGAQTIAHELGHALGFYHDhdrkdrddyptiddtlnaedDDYYSVMSYTKGsFS 148

                       170
                ....*....|....*....
gi 4505209  248 GKSHFMLPDDDVQGIQSLY 266
Cdd:cd00203 149 DGQRKDFSQCDIDQINKLY 167
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 382-428 5.77e-09

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: 51.47  E-value: 5.77e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 4505209     382 ISAAVHFEDtGKTLLFSGNQVWRYDDTNhiMDKDYPRLIEEDFPGIG 428
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGLP 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 32-91 4.35e-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: 49.44  E-value: 4.35e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4505209     32 SEEDLQFAERYLRSY-YHPTNLAGILkenaASSMTERLREMQSFFGLEVTGKLDDNTLDVM 91
Cdd:pfam01471   1 SGEDVKELQRYLNRLgYYPGPVDGYF----GPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 334-376 2.48e-07

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 47.18  E-value: 2.48e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 4505209    334 IDAAYEHPsHDLIFIFRGRKFWALNGYDILEGYPKKISEL-GLP 376
Cdd:pfam00045   1 IDAAFEDR-DGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 334-376 2.75e-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: 44.16  E-value: 2.75e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 4505209     334 IDAAYEHPsHDLIFIFRGRKFWALNGYDILEGYPKKISEL--GLP 376
Cdd:smart00120   1 IDAAFELR-DGKTYFFKGDKYWRFDPKRVDPGYPKLISSFfpGLP 44
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 118-233 3.95e-06

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: 46.72  E-value: 3.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505209  118 LTYRIVNYTPDmthsEVEKAFKKAFKVWSDVTPLNFTRLHDGI-ADIMISFGIKEHGDfypfDGPSGLLAHAFPPGpnyG 196
Cdd:cd04268   4 ITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNANDVDpADIRYSVIRWIPYN----DGTWSYGPSQVDPL---T 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 4505209  197 GDAHfDDDETWTSSSKGYN---LFLVAAHEFGHSLGLDHS 233
Cdd:cd04268  73 GEIL-LARVYLYSSFVEYSgarLRNTAEHELGHALGLRHN 111
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 382-428 4.44e-06

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 43.32  E-value: 4.44e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 4505209    382 ISAAVHFEDtGKTLLFSGNQVWRYDDTNhiMDKDYPRLIeEDFPGIG 428
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQR--VEPGYPKLI-SDFPGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 290-331 1.26e-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: 42.23  E-value: 1.26e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 4505209     290 LDAITSLR-GETMIFKDRFFWRLHPQQVDA-ELFLTKSFWPELP 331
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDPgYPKLISSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 290-317 3.26e-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: 38.32  E-value: 3.26e-04
                          10        20
                  ....*....|....*....|....*....
gi 4505209    290 LDAITSLR-GETMIFKDRFFWRLHPQQVD 317
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVE 29
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 133-232 4.26e-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: 41.60  E-value: 4.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505209  133 EVEKAFKKAFKVWSDVTPLNFTRLHDGIADIMISFgiKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSssk 212
Cdd:cd04327  20 FLKDKVRAAAREWLPYANLKFKFVTDADADIRISF--TPGDGYWSYVGTDALLIGADAPTMNLGWFTDDTPDPEFSR--- 94

                        90       100
                ....*....|....*....|
gi 4505209  213 gynlflVAAHEFGHSLGLDH 232
Cdd:cd04327  95 ------VVLHEFGHALGFIH 108
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
219-242 3.80e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 38.40  E-value: 3.80e-03
                        10        20
                ....*....|....*....|....
gi 4505209  219 VAAHEFGHSLGLDHSKDPGALMFP 242
Cdd:COG1913 126 EAVHELGHLFGLGHCPNPRCVMHF 149
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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