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Conserved domains on  [gi|160333381|ref|NP_032637|]
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neutrophil collagenase preproprotein [Mus musculus]

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 ...
 107-262 8.77e-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: 270.26  E-value: 8.77e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333381  107 KWTHTNLTYRIINHTPQLSRAEVKTAIEKAFHVWSVASPLTFTEILQGEADINIAFVSRDHGDNSPFDGPNGILAHAFQP 186
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160333381  187 GQGIGGDAHFDSEETWTQDSKN---YNLFLVAAHEFGHSLGLSHSTDPGALMYPNYAYREPSTYSLPQDDINGIQTIYG 262
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDPphgINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 276-464 6.96e-74

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: 230.66  E-value: 6.96e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333381 276 PKACDPhLRFDATTTLRGEIYFFKDKYFWRRHPQLRTVDLNFISLFWPFLPNGLQAAYEDFDRDLVFLFKGRQYWALSGY 355
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333381 356 DLQQGYPRDISNYGFPRSVQAIDAAVSY--NGKTYFFINNQCWRYDNQRRSMDPGYPKSIPSMFPGVNCRVDAVFL-QDS 432
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWpdNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLDG 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 160333381 433 FFLFFSGPQYFAFNFVS--HRVTRVARSN-LWLNC 464
Cdd:cd00094  160 YYYFFKGDQYWRFDPRSkeVRVGYPLKISsDWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-86 7.95e-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: 48.67  E-value: 7.95e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 160333381   31 NIKTAENYLRKFYNLPSNQfrSSRNATMVAEKLKEMQRFFSLAETGKLDAATMGIM 86
Cdd:pfam01471   4 DVKELQRYLNRLGYYPGPV--DGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 107-262 8.77e-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: 270.26  E-value: 8.77e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333381  107 KWTHTNLTYRIINHTPQLSRAEVKTAIEKAFHVWSVASPLTFTEILQGEADINIAFVSRDHGDNSPFDGPNGILAHAFQP 186
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160333381  187 GQGIGGDAHFDSEETWTQDSKN---YNLFLVAAHEFGHSLGLSHSTDPGALMYPNYAYREPSTYSLPQDDINGIQTIYG 262
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDPphgINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 107-262 3.75e-79

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: 242.88  E-value: 3.75e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333381 107 KWTHTNLTYRIINHTPQLSRAEVKTAIEKAFHVWSVASPLTFTEILQG-EADINIAFVSRDHGDNSPFDGPNGILAHAFQ 185
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160333381 186 PGqGIGGDAHFDSEETWT--QDSKNYNLFLVAAHEFGHSLGLSHSTDPGALMYPNYAYREPStYSLPQDDINGIQTIYG 262
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTlgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK-FKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 276-464 6.96e-74

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: 230.66  E-value: 6.96e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333381 276 PKACDPhLRFDATTTLRGEIYFFKDKYFWRRHPQLRTVDLNFISLFWPFLPNGLQAAYEDFDRDLVFLFKGRQYWALSGY 355
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333381 356 DLQQGYPRDISNYGFPRSVQAIDAAVSY--NGKTYFFINNQCWRYDNQRRSMDPGYPKSIPSMFPGVNCRVDAVFL-QDS 432
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWpdNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLDG 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 160333381 433 FFLFFSGPQYFAFNFVS--HRVTRVARSN-LWLNC 464
Cdd:cd00094  160 YYYFFKGDQYWRFDPRSkeVRVGYPLKISsDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 104-263 2.48e-33

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: 122.46  E-value: 2.48e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333381   104 GSPKWTHTNLTYRIinHTPQLSRaEVKTAIEKAFHVWSVASPLTFTEIlQGEADINIAFVSRDHGdnsPFdgpngiLAHA 183
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVER-TGTADIYISFGSGDSG---CT------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333381   184 FQPGqgigGDAHFDsEETWTQDSKnynlflVAAHEFGHSLGLSHSTDPGA---LMYPNYAYREPSTYSLPQDDINGIQTI 260
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136


                   ...
gi 160333381   261 YGP 263
Cdd:smart00235 137 YGS 139
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 377-422 6.85e-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: 6.85e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 160333381   377 IDAAVSY-NGKTYFFINNQCWRYDNQRrsMDPGYPKSIPSMFPGVNC 422
Cdd:smart00120   1 IDAAFELrDGKTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGLPC 45
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-86 7.95e-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: 48.67  E-value: 7.95e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 160333381   31 NIKTAENYLRKFYNLPSNQfrSSRNATMVAEKLKEMQRFFSLAETGKLDAATMGIM 86
Cdd:pfam01471   4 DVKELQRYLNRLGYYPGPV--DGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 377-422 8.43e-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: 8.43e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 160333381  377 IDAAVSY-NGKTYFFINNQCWRYDNQRrsMDPGYPKSIPSmFPGVNC 422
Cdd:pfam00045   1 IDAAFEDrDGKTYFFKGRKYWRFDPQR--VEPGYPKLISD-FPGLPC 44
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
208-237 7.01e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 40.33  E-value: 7.01e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 160333381 208 NYNLFL-----VAAHEFGHSLGLSHSTDPGALMYP 237
Cdd:COG1913  115 DEELFLervlkEAVHELGHLFGLGHCPNPRCVMHF 149
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 107-262 8.77e-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: 270.26  E-value: 8.77e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333381  107 KWTHTNLTYRIINHTPQLSRAEVKTAIEKAFHVWSVASPLTFTEILQGEADINIAFVSRDHGDNSPFDGPNGILAHAFQP 186
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160333381  187 GQGIGGDAHFDSEETWTQDSKN---YNLFLVAAHEFGHSLGLSHSTDPGALMYPNYAYREPSTYSLPQDDINGIQTIYG 262
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDPphgINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 107-262 3.75e-79

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: 242.88  E-value: 3.75e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333381 107 KWTHTNLTYRIINHTPQLSRAEVKTAIEKAFHVWSVASPLTFTEILQG-EADINIAFVSRDHGDNSPFDGPNGILAHAFQ 185
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160333381 186 PGqGIGGDAHFDSEETWT--QDSKNYNLFLVAAHEFGHSLGLSHSTDPGALMYPNYAYREPStYSLPQDDINGIQTIYG 262
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTlgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK-FKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 276-464 6.96e-74

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: 230.66  E-value: 6.96e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333381 276 PKACDPhLRFDATTTLRGEIYFFKDKYFWRRHPQLRTVDLNFISLFWPFLPNGLQAAYEDFDRDLVFLFKGRQYWALSGY 355
Cdd:cd00094    1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333381 356 DLQQGYPRDISNYGFPRSVQAIDAAVSY--NGKTYFFINNQCWRYDNQRRSMDPGYPKSIPSMFPGVNCRVDAVFL-QDS 432
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWpdNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLDG 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 160333381 433 FFLFFSGPQYFAFNFVS--HRVTRVARSN-LWLNC 464
Cdd:cd00094  160 YYYFFKGDQYWRFDPRSkeVRVGYPLKISsDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 104-263 2.48e-33

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: 122.46  E-value: 2.48e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333381   104 GSPKWTHTNLTYRIinHTPQLSRaEVKTAIEKAFHVWSVASPLTFTEIlQGEADINIAFVSRDHGdnsPFdgpngiLAHA 183
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVER-TGTADIYISFGSGDSG---CT------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333381   184 FQPGqgigGDAHFDsEETWTQDSKnynlflVAAHEFGHSLGLSHSTDPGA---LMYPNYAYREPSTYSLPQDDINGIQTI 260
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136


                   ...
gi 160333381   261 YGP 263
Cdd:smart00235 137 YGS 139
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 128-262 9.58e-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: 77.11  E-value: 9.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333381 128 EVKTAIEKAFHVWSVASPLTFTEI--LQGEADINIAFVSRDHGDNSPfdgpnGILAHAFQPGQGIGGDAHFDSEE---TW 202
Cdd:cd04279   21 SWLQAVKQAAAEWENVGPLKFVYNpeEDNDADIVIFFDRPPPVGGAG-----GGLARAGFPLISDGNRKLFNRTDinlGP 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160333381 203 TQDSKNYNLFLVAAHEFGHSLGLSHSTD-PGALMYPNYAYREPSTYSLPQDDINGIQTIYG 262
Cdd:cd04279   96 GQPRGAENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 104-262 1.11e-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: 72.06  E-value: 1.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333381 104 GSPKWTHTNLTYRIINHTPQLSrAEVKTAIEKAFHVWSVASPLTFTEILQGE-ADINIAFVSRDHGDNspfdgpngiLAH 182
Cdd:cd04277   11 TGGPYSYGYGREEDTTNTAALS-AAQQAAARDALEAWEDVADIDFVEVSDNSgADIRFGNSSDPDGNT---------AGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333381 183 AFQPG----QGIGGDAHFDSEETWTQDSK-NYNlFLVAAHEFGHSLGLSHSTDPGA----------------LM------ 235
Cdd:cd04277   81 AYYPGsgsgTAYGGDIWFNSSYDTNSDSPgSYG-YQTIIHEIGHALGLEHPGDYNGgdpvpptyaldsreytVMsynsgy 159

                        170       180
                 ....*....|....*....|....*....
gi 160333381 236 --YPNYAYREPSTYSLpqDDINGIQTIYG 262
Cdd:cd04277  160 gnGASAGGGYPQTPML--LDIAALQYLYG 186
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 377-422 6.85e-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: 6.85e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 160333381   377 IDAAVSY-NGKTYFFINNQCWRYDNQRrsMDPGYPKSIPSMFPGVNC 422
Cdd:smart00120   1 IDAAFELrDGKTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGLPC 45
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 123-261 1.18e-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: 60.23  E-value: 1.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333381 123 QLSRAEVKTAIEKAFHVWSVASPLTFTEILQGEADINIAFVsrdhgdNSPFDGPNGILAHAFQPG--QGIGGDAHFDSEE 200
Cdd:cd00203   17 ENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIDKADIAIL------VTRQDFDGGTGGWAYLGRvcDSLRGVGVLQDNQ 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333381 201 TWtqdskNYNLFLVAAHEFGHSLGLSHS--------------------TDPGALMYPnYAYREPSTYSLP--QDDINGIQ 258
Cdd:cd00203   91 SG-----TKEGAQTIAHELGHALGFYHDhdrkdrddyptiddtlnaedDDYYSVMSY-TKGSFSDGQRKDfsQCDIDQIN 164


                 ...
gi 160333381 259 TIY 261
Cdd:cd00203  165 KLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 113-261 3.77e-08

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: 52.88  E-value: 3.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333381 113 LTYRIINHTPQlsraEVKTAIEKAFHVWSVASPLTFTE-ILQGEADINIAFVSrdhgDNSPFDGPNGILAHAFQPGQGIG 191
Cdd:cd04268    4 ITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNaNDVDPADIRYSVIR----WIPYNDGTWSYGPSQVDPLTGEI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333381 192 GDAHFDSEETWTQDSKNYnLFLVAAHEFGHSLGLSHS----------------TDPGALMYP---NYAYREP--STYSLP 250
Cdd:cd04268   76 LLARVYLYSSFVEYSGAR-LRNTAEHELGHALGLRHNfaasdrddnvdllaekGDTSSVMDYapsNFSIQLGdgQKYTIG 154

                        170
                 ....*....|.
gi 160333381 251 QDDINGIQTIY 261
Cdd:cd04268  155 PYDIAAIKKLY 165
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 31-86 7.95e-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: 48.67  E-value: 7.95e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 160333381   31 NIKTAENYLRKFYNLPSNQfrSSRNATMVAEKLKEMQRFFSLAETGKLDAATMGIM 86
Cdd:pfam01471   4 DVKELQRYLNRLGYYPGPV--DGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 377-422 8.43e-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: 8.43e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 160333381  377 IDAAVSY-NGKTYFFINNQCWRYDNQRrsMDPGYPKSIPSmFPGVNC 422
Cdd:pfam00045   1 IDAAFEDrDGKTYFFKGRKYWRFDPQR--VEPGYPKLISD-FPGLPC 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 329-371 1.45e-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: 47.56  E-value: 1.45e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 160333381  329 LQAAYEDfDRDLVFLFKGRQYWALSGYDLQQGYPRDISNY-GFP 371
Cdd:pfam00045   1 IDAAFED-RDGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 285-326 8.77e-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: 8.77e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 160333381   285 FDATTTLR-GEIYFFKDKYFWRRHPQ-LRTVDLNFISLFWPFLP 326
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKrVDPGYPKLISSFFPGLP 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 329-372 2.23e-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: 2.23e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 160333381   329 LQAAYEDfDRDLVFLFKGRQYWALSGYDLQQGYPRDISNY--GFPR 372
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFfpGLPC 45
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 127-227 1.19e-05

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: 45.83  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333381 127 AEVKTAIEKAFHVWSVASPLTFTEILQGEADINIAFvsRDHGDNSPFDGPNGILAHAFQPGQGIGGDAHFDSEETWTQds 206
Cdd:cd04327   19 AFLKDKVRAAAREWLPYANLKFKFVTDADADIRISF--TPGDGYWSYVGTDALLIGADAPTMNLGWFTDDTPDPEFSR-- 94

                         90       100
                 ....*....|....*....|.
gi 160333381 207 knynlflVAAHEFGHSLGLSH 227
Cdd:cd04327   95 -------VVLHEFGHALGFIH 108
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 285-327 2.97e-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: 2.97e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 160333381  285 FDATTTLR-GEIYFFKDKYFWRRHPQ-LRTVDLNFISLFwPFLPN 327
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQrVEPGYPKLISDF-PGLPC 44
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
208-237 7.01e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 40.33  E-value: 7.01e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 160333381 208 NYNLFL-----VAAHEFGHSLGLSHSTDPGALMYP 237
Cdd:COG1913  115 DEELFLervlkEAVHELGHLFGLGHCPNPRCVMHF 149
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
144-264 1.22e-03

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 40.09  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333381  144 SPLTFTEILQgEADINIAFVSRDHGDN----SPFDGPNGILAHAFQP-GQGIGGDAHFDSEETwTQDSKNYNLFLVAAHE 218
Cdd:pfam13688  67 STGDSSDRLS-EFQDFSAWRGTQNDDLaylfLMTNCSGGGLAWLGQLcNSGSAGSVSTRVSGN-NVVVSTATEWQVFAHE 144

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 160333381  219 FGHSLGLSHstDPGAlmYPNYAYREPSTYSLPqddiNGIQTIYGPS 264
Cdd:pfam13688 145 IGHNFGAVH--DCDS--STSSQCCPPSNSTCP----AGGRYIMNPS 182
 
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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