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Conserved domains on  [gi|4505215|ref|NP_002412|]
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interstitial collagenase isoform 1 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 ...
 108-261 3.35e-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: 271.41  E-value: 3.35e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505215    108 RWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQP 187
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505215    188 GPGIGGDAHFDEDERWT---NNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSY--TFSGDVQLAQDDIDGIQAIYG 261
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTvgsDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYspLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 275-466 2.65e-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: 257.63  E-value: 2.65e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505215  275 PKACDSkLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFISVFWPQLPNGLEAAYEFADRDEVRFFKGNKYWAVQGQ 354
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505215  355 NVLHGYPKDIYsSFGFPRTVKHIDAALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDFPGIGHKVDAVFM-KD 433
Cdd:cd00094  80 NLEPGYPKPIS-DLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLD 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 4505215  434 GFFYFFHGTRQYKFDPKTK--RILTLQKANS-WFNC 466
Cdd:cd00094 159 GYYYFFKGDQYWRFDPRSKevRVGYPLKISSdWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 27-87 1.87e-10

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


:

Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 56.37  E-value: 1.87e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4505215     27 QEQDVDLVQKYLEK--YYNLKNDGRqvekrrnSGP-VVEKLKQMQEFFGLKVTGKPDAETLKVM 87
Cdd:pfam01471   1 SGEDVKELQRYLNRlgYYPGPVDGY-------FGPsTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 108-261 3.35e-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: 271.41  E-value: 3.35e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505215    108 RWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQP 187
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505215    188 GPGIGGDAHFDEDERWT---NNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSY--TFSGDVQLAQDDIDGIQAIYG 261
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTvgsDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYspLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 275-466 2.65e-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: 257.63  E-value: 2.65e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505215  275 PKACDSkLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFISVFWPQLPNGLEAAYEFADRDEVRFFKGNKYWAVQGQ 354
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505215  355 NVLHGYPKDIYsSFGFPRTVKHIDAALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDFPGIGHKVDAVFM-KD 433
Cdd:cd00094  80 NLEPGYPKPIS-DLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLD 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 4505215  434 GFFYFFHGTRQYKFDPKTK--RILTLQKANS-WFNC 466
Cdd:cd00094 159 GYYYFFKGDQYWRFDPRSKevRVGYPLKISSdWLGC 194
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 108-261 3.60e-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: 240.57  E-value: 3.60e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505215  108 RWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKV-SEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQ 186
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4505215  187 PGpGIGGDAHFDEDERWT--NNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSYTFS-GDVQLAQDDIDGIQAIYG 261
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTlgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPvPKFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 105-261 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: 120.92  E-value: 1.32e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505215     105 GNPRWEQTHLTYRIenYTPDLPRaDVDHAIEKAFQLWSNVTPLTFTKVSEGqADIMISFVRGDHrdnspfdgpGGNLAHA 184
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDS---------GCTLSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505215     185 FQPGpgigGDAHFDeDERWTNNFReynlhrVAAHELGHSLGLSHSTDIGA---LMYPSYTF--SGDVQLAQDDIDGIQAI 259
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNidTRNFDLSEDDSLGIPYD 136


                   ..
gi 4505215     260 YG 261
Cdd:smart00235 137 YG 138
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 377-424 3.32e-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: 58.02  E-value: 3.32e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 4505215     377 IDAALSEENtGKTYFFVANKYWRYDEYKrsMDPGYPKMIAHDFPGIGH 424
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGLPC 45
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 27-87 1.87e-10

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 56.37  E-value: 1.87e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4505215     27 QEQDVDLVQKYLEK--YYNLKNDGRqvekrrnSGP-VVEKLKQMQEFFGLKVTGKPDAETLKVM 87
Cdd:pfam01471   1 SGEDVKELQRYLNRlgYYPGPVDGY-------FGPsTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 377-424 4.75e-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: 54.88  E-value: 4.75e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 4505215    377 IDAALsEENTGKTYFFVANKYWRYDEYKrsMDPGYPKMIAhDFPGIGH 424
Cdd:pfam00045   1 IDAAF-EDRDGKTYFFKGRKYWRFDPQR--VEPGYPKLIS-DFPGLPC 44
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
215-239 7.29e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 40.33  E-value: 7.29e-04
                        10        20
                ....*....|....*....|....*
gi 4505215  215 VAAHELGHSLGLSHSTDIGALMYPS 239
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 ...
 108-261 3.35e-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: 271.41  E-value: 3.35e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505215    108 RWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQP 187
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505215    188 GPGIGGDAHFDEDERWT---NNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSY--TFSGDVQLAQDDIDGIQAIYG 261
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTvgsDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYspLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 275-466 2.65e-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: 257.63  E-value: 2.65e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505215  275 PKACDSkLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFISVFWPQLPNGLEAAYEFADRDEVRFFKGNKYWAVQGQ 354
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505215  355 NVLHGYPKDIYsSFGFPRTVKHIDAALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDFPGIGHKVDAVFM-KD 433
Cdd:cd00094  80 NLEPGYPKPIS-DLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLD 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 4505215  434 GFFYFFHGTRQYKFDPKTK--RILTLQKANS-WFNC 466
Cdd:cd00094 159 GYYYFFKGDQYWRFDPRSKevRVGYPLKISSdWLGC 194
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 108-261 3.60e-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: 240.57  E-value: 3.60e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505215  108 RWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKV-SEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQ 186
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4505215  187 PGpGIGGDAHFDEDERWT--NNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSYTFS-GDVQLAQDDIDGIQAIYG 261
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTlgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPvPKFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 105-261 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: 120.92  E-value: 1.32e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505215     105 GNPRWEQTHLTYRIenYTPDLPRaDVDHAIEKAFQLWSNVTPLTFTKVSEGqADIMISFVRGDHrdnspfdgpGGNLAHA 184
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDS---------GCTLSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505215     185 FQPGpgigGDAHFDeDERWTNNFReynlhrVAAHELGHSLGLSHSTDIGA---LMYPSYTF--SGDVQLAQDDIDGIQAI 259
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNidTRNFDLSEDDSLGIPYD 136


                   ..
gi 4505215     260 YG 261
Cdd:smart00235 137 YG 138
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 133-261 1.90e-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: 79.42  E-value: 1.90e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505215  133 AIEKAFQLWSNVTPLTFTKVSEG--QADIMISFVRGDHRDNSpfdgpGGNLAHAFQPGPGIGGDA---HFDEDERWTNNF 207
Cdd:cd04279  25 AVKQAAAEWENVGPLKFVYNPEEdnDADIVIFFDRPPPVGGA-----GGGLARAGFPLISDGNRKlfnRTDINLGPGQPR 99

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4505215  208 REYNLHRVAAHELGHSLGLSHSTDIGA-LMYPSY--TFSGDVQLAQDDIDGIQAIYG 261
Cdd:cd04279 100 GAENLQAIALHELGHALGLWHHSDRPEdAMYPSQgqGPDGNPTLSARDVATLKRLYG 156
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 124-260 3.17e-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: 73.33  E-value: 3.17e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505215  124 DLPRADVDHAIEKAFQLWSNVTPLTFTKVSEG--QADIMISFVRGDhrdnspFDGPGGNLAHAFQPGPGIGGDAHFDEDE 201
Cdd:cd00203  17 ENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEidKADIAILVTRQD------FDGGTGGWAYLGRVCDSLRGVGVLQDNQ 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505215  202 RWTNNFreynlHRVAAHELGHSLGLSHS--------------------TDIGALMYPSYTFSGDVQ---LAQDDIDGIQA 258
Cdd:cd00203  91 SGTKEG-----AQTIAHELGHALGFYHDhdrkdrddyptiddtlnaedDDYYSVMSYTKGSFSDGQrkdFSQCDIDQINK 165


                ..
gi 4505215  259 IY 260
Cdd:cd00203 166 LY 167
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 132-261 2.50e-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: 71.29  E-value: 2.50e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505215  132 HAIEKAFQLWSNVTPLTFTKVSEGQ-ADIMISFvrgdhrdnspFDGP-GGNLAHAFQPGPGI----GGDAHFDEDERWTN 205
Cdd:cd04277  37 AAARDALEAWEDVADIDFVEVSDNSgADIRFGN----------SSDPdGNTAGYAYYPGSGSgtayGGDIWFNSSYDTNS 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505215  206 NFRE-YNLHrVAAHELGHSLGLSHSTDIGA----------------LM------YPSYTFSGDVQLA--QDDIDGIQAIY 260
Cdd:cd04277 107 DSPGsYGYQ-TIIHEIGHALGLEHPGDYNGgdpvpptyaldsreytVMsynsgyGNGASAGGGYPQTpmLLDIAALQYLY 185


                .
gi 4505215  261 G 261
Cdd:cd04277 186 G 186
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 114-260 2.94e-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: 61.74  E-value: 2.94e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505215  114 LTYRIENYTPDlpraDVDHAIEKAFQLWSNVTPLTFTKVSEG-QADIMISFVRGDHRDNspfdgpGGNLAHAFQPGPGiG 192
Cdd:cd04268   4 ITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNANDVdPADIRYSVIRWIPYND------GTWSYGPSQVDPL-T 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505215  193 GDAHFDeDERWTNNFREYN---LHRVAAHELGHSLGLSHS----------------TDIGALM-YPSYTFSGDVQLAQ-- 250
Cdd:cd04268  73 GEILLA-RVYLYSSFVEYSgarLRNTAEHELGHALGLRHNfaasdrddnvdllaekGDTSSVMdYAPSNFSIQLGDGQky 151

                       170
                ....*....|....
gi 4505215  251 ----DDIDGIQAIY 260
Cdd:cd04268 152 tigpYDIAAIKKLY 165
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 377-424 3.32e-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: 58.02  E-value: 3.32e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 4505215     377 IDAALSEENtGKTYFFVANKYWRYDEYKrsMDPGYPKMIAHDFPGIGH 424
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGLPC 45
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 27-87 1.87e-10

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 56.37  E-value: 1.87e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4505215     27 QEQDVDLVQKYLEK--YYNLKNDGRqvekrrnSGP-VVEKLKQMQEFFGLKVTGKPDAETLKVM 87
Cdd:pfam01471   1 SGEDVKELQRYLNRlgYYPGPVDGY-------FGPsTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 377-424 4.75e-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: 54.88  E-value: 4.75e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 4505215    377 IDAALsEENTGKTYFFVANKYWRYDEYKrsMDPGYPKMIAhDFPGIGH 424
Cdd:pfam00045   1 IDAAF-EDRDGKTYFFKGRKYWRFDPQR--VEPGYPKLIS-DFPGLPC 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 328-371 6.03e-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: 48.72  E-value: 6.03e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 4505215    328 LEAAYEFaDRDEVRFFKGNKYWAVQGQNVLHGYPKDIYSSFGFP 371
Cdd:pfam00045   1 IDAAFED-RDGKTYFFKGRKYWRFDPQRVEPGYPKLISDFPGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 330-372 5.98e-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: 46.08  E-value: 5.98e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 4505215     330 AAYEFaDRDEVRFFKGNKYWAVQGQNVLHGYPKDIYSSF-GFPR 372
Cdd:smart00120   3 AAFEL-RDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFpGLPC 45
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 284-325 5.69e-05

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 40.30  E-value: 5.69e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 4505215     284 FDAITTIR-GEVMFFKDRFYMRTNPFYPE-VELNFISVFWPQLP 325
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKRVDpGYPKLISSFFPGLP 44
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
215-239 7.29e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 40.33  E-value: 7.29e-04
                        10        20
                ....*....|....*....|....*
gi 4505215  215 VAAHELGHSLGLSHSTDIGALMYPS 239
Cdd:COG1913 126 EAVHELGHLFGLGHCPNPRCVMHFS 150
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 197-241 1.22e-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: 1.22e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 4505215  197 FDEDERWTNNFREyNLHRVAAHELGHSLGLSHSTDIGALMYPSYT 241
Cdd:cd11375 109 FYGLPPDEGLFLE-RLLKEAVHELGHLFGLDHCPYYACVMNFSNS 152
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 426-451 1.93e-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: 36.01  E-value: 1.93e-03
                          10        20
                  ....*....|....*....|....*..
gi 4505215    426 VDAVFM-KDGFFYFFHGTRQYKFDPKT 451
Cdd:pfam00045   1 IDAAFEdRDGKTYFFKGRKYWRFDPQR 27
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 126-228 2.79e-03

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


Pssm-ID: 239819 [Multi-domain]  Cd Length: 198  Bit Score: 38.90  E-value: 2.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505215  126 PRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDhrDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDerwtN 205
Cdd:cd04327  17 PDAFLKDKVRAAAREWLPYANLKFKFVTDADADIRISFTPGD--GYWSYVGTDALLIGADAPTMNLGWFTDDTPD----P 90

                        90       100
                ....*....|....*....|...
gi 4505215  206 NFReynlhRVAAHELGHSLGLSH 228
Cdd:cd04327  91 EFS-----RVVLHEFGHALGFIH 108
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 426-451 3.77e-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: 35.30  E-value: 3.77e-03
                           10        20
                   ....*....|....*....|....*..
gi 4505215     426 VDAVF-MKDGFFYFFHGTRQYKFDPKT 451
Cdd:smart00120   1 IDAAFeLRDGKTYFFKGDKYWRFDPKR 27
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 214-261 4.52e-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: 4.52e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4505215  214 RVAAHELGHSLGLSHSTDIGA----------LMYPSYTFSGDVQLAQDDIDGIQAIYG 261
Cdd:cd04267 135 LTMAHELGHNLGAEHDGGDELafecdgggnyIMAPVDSGLNSYRFSQCSIGSIREFLD 192
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 284-326 6.55e-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: 34.46  E-value: 6.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 4505215    284 FDAITTIR-GEVMFFKDRFYMRTNPFYPE-VELNFISVFwPQLPN 326
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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