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Conserved domains on  [gi|225543094|ref|NP_001139410|]
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interstitial collagenase isoform 2 [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 ...
42-195 3.16e-90

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: 269.10  E-value: 3.16e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543094   42 RWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQP 121
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225543094  122 GPGIGGDAHFDEDERWT---NNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSY--TFSGDVQLAQDDIDGIQAIYG 195
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTvgsDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYspLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
209-400 3.71e-84

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: 254.93  E-value: 3.71e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543094 209 PKACDSkLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFISVFWPQLPNGLEAAYEFADRDEVRFFKGNKYWAVQGQ 288
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543094 289 NVLHGYPKDIYsSFGFPRTVKHIDAALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDFPGIGHKVDAVFM-KD 367
Cdd:cd00094   80 NLEPGYPKPIS-DLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLD 158
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 225543094 368 GFFYFFHGTRQYKFDPKTK--RILTLQKANS-WFNC 400
Cdd:cd00094  159 GYYYFFKGDQYWRFDPRSKevRVGYPLKISSdWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
1-21 2.33e-04

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: 38.65  E-value: 2.33e-04
                          10        20
                  ....*....|....*....|.
gi 225543094    1 MQEFFGLKVTGKPDAETLKVM 21
Cdd:pfam01471  37 FQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
42-195 3.16e-90

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: 269.10  E-value: 3.16e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543094   42 RWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQP 121
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225543094  122 GPGIGGDAHFDEDERWT---NNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSY--TFSGDVQLAQDDIDGIQAIYG 195
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTvgsDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYspLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
209-400 3.71e-84

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: 254.93  E-value: 3.71e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543094 209 PKACDSkLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFISVFWPQLPNGLEAAYEFADRDEVRFFKGNKYWAVQGQ 288
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543094 289 NVLHGYPKDIYsSFGFPRTVKHIDAALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDFPGIGHKVDAVFM-KD 367
Cdd:cd00094   80 NLEPGYPKPIS-DLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLD 158
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 225543094 368 GFFYFFHGTRQYKFDPKTK--RILTLQKANS-WFNC 400
Cdd:cd00094  159 GYYYFFKGDQYWRFDPRSKevRVGYPLKISSdWLGC 194
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
42-195 3.23e-78

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: 238.26  E-value: 3.23e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543094  42 RWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKV-SEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQ 120
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225543094 121 PGpGIGGDAHFDEDERWT--NNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSYTFS-GDVQLAQDDIDGIQAIYG 195
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTlgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPvPKFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
39-195 1.32e-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: 119.76  E-value: 1.32e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543094    39 GNPRWEQTHLTYRIenYTPDLPRaDVDHAIEKAFQLWSNVTPLTFTKVSEGqADIMISFVRGDHrdnspfdgpGGNLAHA 118
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDS---------GCTLSHA 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543094   119 FQPGpgigGDAHFDeDERWTNNFReynlhrVAAHELGHSLGLSHSTDIGA---LMYPSYTF--SGDVQLAQDDIDGIQAI 193
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNidTRNFDLSEDDSLGIPYD 136

                   ..
gi 225543094   194 YG 195
Cdd:smart00235 137 YG 138
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
311-358 5.20e-11

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: 57.25  E-value: 5.20e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 225543094   311 IDAALSEENtGKTYFFVANKYWRYDEYKrsMDPGYPKMIAHDFPGIGH 358
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
311-358 7.25e-10

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 54.11  E-value: 7.25e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 225543094  311 IDAALsEENTGKTYFFVANKYWRYDEYKrsMDPGYPKMIAhDFPGIGH 358
Cdd:pfam00045   1 IDAAF-EDRDGKTYFFKGRKYWRFDPQR--VEPGYPKLIS-DFPGLPC 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
1-21 2.33e-04

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: 38.65  E-value: 2.33e-04
                          10        20
                  ....*....|....*....|.
gi 225543094    1 MQEFFGLKVTGKPDAETLKVM 21
Cdd:pfam01471  37 FQRAFGLPVDGIVDPETLAAL 57
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
149-173 6.01e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 40.33  E-value: 6.01e-04
                         10        20
                 ....*....|....*....|....*
gi 225543094 149 VAAHELGHSLGLSHSTDIGALMYPS 173
Cdd:COG1913  126 EAVHELGHLFGLGHCPNPRCVMHFS 150
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
42-195 3.16e-90

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: 269.10  E-value: 3.16e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543094   42 RWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQP 121
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225543094  122 GPGIGGDAHFDEDERWT---NNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSY--TFSGDVQLAQDDIDGIQAIYG 195
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTvgsDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYspLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
209-400 3.71e-84

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: 254.93  E-value: 3.71e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543094 209 PKACDSkLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFISVFWPQLPNGLEAAYEFADRDEVRFFKGNKYWAVQGQ 288
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543094 289 NVLHGYPKDIYsSFGFPRTVKHIDAALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDFPGIGHKVDAVFM-KD 367
Cdd:cd00094   80 NLEPGYPKPIS-DLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLD 158
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 225543094 368 GFFYFFHGTRQYKFDPKTK--RILTLQKANS-WFNC 400
Cdd:cd00094  159 GYYYFFKGDQYWRFDPRSKevRVGYPLKISSdWLGC 194
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
42-195 3.23e-78

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: 238.26  E-value: 3.23e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543094  42 RWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKV-SEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQ 120
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225543094 121 PGpGIGGDAHFDEDERWT--NNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSYTFS-GDVQLAQDDIDGIQAIYG 195
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTlgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPvPKFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
39-195 1.32e-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: 119.76  E-value: 1.32e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543094    39 GNPRWEQTHLTYRIenYTPDLPRaDVDHAIEKAFQLWSNVTPLTFTKVSEGqADIMISFVRGDHrdnspfdgpGGNLAHA 118
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDS---------GCTLSHA 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543094   119 FQPGpgigGDAHFDeDERWTNNFReynlhrVAAHELGHSLGLSHSTDIGA---LMYPSYTF--SGDVQLAQDDIDGIQAI 193
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNidTRNFDLSEDDSLGIPYD 136

                   ..
gi 225543094   194 YG 195
Cdd:smart00235 137 YG 138
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
67-195 1.54e-17

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: 79.04  E-value: 1.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543094  67 AIEKAFQLWSNVTPLTFTKVSEG--QADIMISFVRGDHRDNSpfdgpGGNLAHAFQPGPGIGGDA---HFDEDERWTNNF 141
Cdd:cd04279   25 AVKQAAAEWENVGPLKFVYNPEEdnDADIVIFFDRPPPVGGA-----GGGLARAGFPLISDGNRKlfnRTDINLGPGQPR 99
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 225543094 142 REYNLHRVAAHELGHSLGLSHSTDIGA-LMYPSY--TFSGDVQLAQDDIDGIQAIYG 195
Cdd:cd04279  100 GAENLQAIALHELGHALGLWHHSDRPEdAMYPSQgqGPDGNPTLSARDVATLKRLYG 156
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
58-194 3.87e-15

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: 72.55  E-value: 3.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543094  58 DLPRADVDHAIEKAFQLWSNVTPLTFTKVSEG--QADIMISFVRGDhrdnspFDGPGGNLAHAFQPGPGIGGDAHFDEDE 135
Cdd:cd00203   17 ENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEidKADIAILVTRQD------FDGGTGGWAYLGRVCDSLRGVGVLQDNQ 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543094 136 RWTNNFreynlHRVAAHELGHSLGLSHS--------------------TDIGALMYPSYTFSGDVQ---LAQDDIDGIQA 192
Cdd:cd00203   91 SGTKEG-----AQTIAHELGHALGFYHDhdrkdrddyptiddtlnaedDDYYSVMSYTKGSFSDGQrkdFSQCDIDQINK 165

                 ..
gi 225543094 193 IY 194
Cdd:cd00203  166 LY 167
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
66-195 6.29e-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: 69.75  E-value: 6.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543094  66 HAIEKAFQLWSNVTPLTFTKVSEGQ-ADIMISFvrgdhrdnspFDGP-GGNLAHAFQPGPGI----GGDAHFDEDERWTN 139
Cdd:cd04277   37 AAARDALEAWEDVADIDFVEVSDNSgADIRFGN----------SSDPdGNTAGYAYYPGSGSgtayGGDIWFNSSYDTNS 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543094 140 NFRE-YNLHrVAAHELGHSLGLSHSTDIGA----------------LM------YPSYTFSGDVQLA--QDDIDGIQAIY 194
Cdd:cd04277  107 DSPGsYGYQ-TIIHEIGHALGLEHPGDYNGgdpvpptyaldsreytVMsynsgyGNGASAGGGYPQTpmLLDIAALQYLY 185

                 .
gi 225543094 195 G 195
Cdd:cd04277  186 G 186
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
48-194 3.51e-11

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


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 61.36  E-value: 3.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543094  48 LTYRIENYTPDlpraDVDHAIEKAFQLWSNVTPLTFTKVSEG-QADIMISFVRGDHRDNspfdgpGGNLAHAFQPGPGiG 126
Cdd:cd04268    4 ITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNANDVdPADIRYSVIRWIPYND------GTWSYGPSQVDPL-T 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543094 127 GDAHFDeDERWTNNFREYN---LHRVAAHELGHSLGLSHS----------------TDIGALM-YPSYTFSGDVQLAQ-- 184
Cdd:cd04268   73 GEILLA-RVYLYSSFVEYSgarLRNTAEHELGHALGLRHNfaasdrddnvdllaekGDTSSVMdYAPSNFSIQLGDGQky 151
                        170
                 ....*....|....
gi 225543094 185 ----DDIDGIQAIY 194
Cdd:cd04268  152 tigpYDIAAIKKLY 165
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
311-358 5.20e-11

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: 57.25  E-value: 5.20e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 225543094   311 IDAALSEENtGKTYFFVANKYWRYDEYKrsMDPGYPKMIAHDFPGIGH 358
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
311-358 7.25e-10

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 54.11  E-value: 7.25e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 225543094  311 IDAALsEENTGKTYFFVANKYWRYDEYKrsMDPGYPKMIAhDFPGIGH 358
Cdd:pfam00045   1 IDAAF-EDRDGKTYFFKGRKYWRFDPQR--VEPGYPKLIS-DFPGLPC 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
262-305 7.90e-08

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: 48.33  E-value: 7.90e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 225543094  262 LEAAYEFaDRDEVRFFKGNKYWAVQGQNVLHGYPKDIYSSFGFP 305
Cdd:pfam00045   1 IDAAFED-RDGKTYFFKGRKYWRFDPQRVEPGYPKLISDFPGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
264-306 8.22e-07

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 45.31  E-value: 8.22e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 225543094   264 AAYEFaDRDEVRFFKGNKYWAVQGQNVLHGYPKDIYSSF-GFPR 306
Cdd:smart00120   3 AAFEL-RDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFpGLPC 45
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
218-259 7.75e-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: 39.92  E-value: 7.75e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 225543094   218 FDAITTIR-GEVMFFKDRFYMRTNPFYPE-VELNFISVFWPQLP 259
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDpGYPKLISSFFPGLP 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
1-21 2.33e-04

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: 38.65  E-value: 2.33e-04
                          10        20
                  ....*....|....*....|.
gi 225543094    1 MQEFFGLKVTGKPDAETLKVM 21
Cdd:pfam01471  37 FQRAFGLPVDGIVDPETLAAL 57
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
149-173 6.01e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 40.33  E-value: 6.01e-04
                         10        20
                 ....*....|....*....|....*
gi 225543094 149 VAAHELGHSLGLSHSTDIGALMYPS 173
Cdd:COG1913  126 EAVHELGHLFGLGHCPNPRCVMHFS 150
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
131-175 1.13e-03

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: 39.59  E-value: 1.13e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 225543094 131 FDEDERWTNNFREyNLHRVAAHELGHSLGLSHSTDIGALMYPSYT 175
Cdd:cd11375  109 FYGLPPDEGLFLE-RLLKEAVHELGHLFGLDHCPYYACVMNFSNS 152
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
360-385 2.29e-03

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: 35.62  E-value: 2.29e-03
                          10        20
                  ....*....|....*....|....*..
gi 225543094  360 VDAVFM-KDGFFYFFHGTRQYKFDPKT 385
Cdd:pfam00045   1 IDAAFEdRDGKTYFFKGRKYWRFDPQR 27
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
60-162 2.88e-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: 38.52  E-value: 2.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543094  60 PRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDhrDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDerwtN 139
Cdd:cd04327   17 PDAFLKDKVRAAAREWLPYANLKFKFVTDADADIRISFTPGD--GYWSYVGTDALLIGADAPTMNLGWFTDDTPD----P 90
                         90       100
                 ....*....|....*....|...
gi 225543094 140 NFReynlhRVAAHELGHSLGLSH 162
Cdd:cd04327   91 EFS-----RVVLHEFGHALGFIH 108
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
148-195 3.71e-03

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: 38.17  E-value: 3.71e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 225543094 148 RVAAHELGHSLGLSHSTDIGA----------LMYPSYTFSGDVQLAQDDIDGIQAIYG 195
Cdd:cd04267  135 LTMAHELGHNLGAEHDGGDELafecdgggnyIMAPVDSGLNSYRFSQCSIGSIREFLD 192
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
360-385 4.66e-03

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 34.91  E-value: 4.66e-03
                           10        20
                   ....*....|....*....|....*..
gi 225543094   360 VDAVF-MKDGFFYFFHGTRQYKFDPKT 385
Cdd:smart00120   1 IDAAFeLRDGKTYFFKGDKYWRFDPKR 27
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
218-260 8.01e-03

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: 34.08  E-value: 8.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 225543094  218 FDAITTIR-GEVMFFKDRFYMRTNPFYPE-VELNFISVFwPQLPN 260
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQRVEpGYPKLISDF-PGLPC 44
 
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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