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Conserved domains on  [gi|2309512006|ref|NP_071557|]
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neutrophil collagenase preproprotein [Rattus norvegicus]

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 ...
 108-263 3.57e-87

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: 263.32  E-value: 3.57e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309512006 108 KWTHTNLTYRIINHTPQMSKAEVKTEIEKAFKIWSVPSTLTFTETLEGEADINIAFVSRDHGDNSPFDGPNGILAHAFQP 187
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2309512006 188 GRGIGGDAHFDSEETWTQDSNN---YNLFLVAAHEFGHSLGLSHSTDPGALMYPNYAYREPSTYSLPQDDINGIQTIYG 263
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDPphgINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 277-465 3.15e-75

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: 234.13  E-value: 3.15e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309512006 277 PTACDPhLRFDAATTLRGEIYFFKDKYFWRRHPQLRTVDLNFISLFWPFLPNGLQAAYEDFDRDLVFLFKGRQYWALSAY 356
Cdd:cd00094     1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309512006 357 DLQQGYPRDISNYGFPRSVQAIDAAVSY--NGKTYFFVNNQCWRYDNQRRSMDPGYPTSIASVFPGINCRIDAVFQ-QDS 433
Cdd:cd00094    80 NLEPGYPKPISDLGFPPTVKQIDAALRWpdNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLDG 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2309512006 434 FFLFFSGPQYFAFNLVSR--RVTRVARSN-LWLNC 465
Cdd:cd00094   160 YYYFFKGDQYWRFDPRSKevRVGYPLKISsDWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 32-87 6.13e-09

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: 51.75  E-value: 6.13e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2309512006  32 NMKTAENYLRKFYHLPSNQfrSARNATMIAEKLKEMQRFFGLPETGKPDAATIEIM 87
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 ...
 108-263 3.57e-87

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: 263.32  E-value: 3.57e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309512006 108 KWTHTNLTYRIINHTPQMSKAEVKTEIEKAFKIWSVPSTLTFTETLEGEADINIAFVSRDHGDNSPFDGPNGILAHAFQP 187
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2309512006 188 GRGIGGDAHFDSEETWTQDSNN---YNLFLVAAHEFGHSLGLSHSTDPGALMYPNYAYREPSTYSLPQDDINGIQTIYG 263
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDPphgINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 108-263 2.35e-76

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: 235.56  E-value: 2.35e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309512006 108 KWTHTNLTYRIINHTPQMSKAEVKTEIEKAFKIWSVPSTLTFTETLEG-EADINIAFVSRDHGDNSPFDGPNGILAHAFQ 186
Cdd:cd04278     1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2309512006 187 PGrGIGGDAHFDSEETWT--QDSNNYNLFLVAAHEFGHSLGLSHSTDPGALMYPNYAYREPStYSLPQDDINGIQTIYG 263
Cdd:cd04278    81 PG-GIGGDIHFDDDEQWTlgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK-FKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 277-465 3.15e-75

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: 234.13  E-value: 3.15e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309512006 277 PTACDPhLRFDAATTLRGEIYFFKDKYFWRRHPQLRTVDLNFISLFWPFLPNGLQAAYEDFDRDLVFLFKGRQYWALSAY 356
Cdd:cd00094     1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309512006 357 DLQQGYPRDISNYGFPRSVQAIDAAVSY--NGKTYFFVNNQCWRYDNQRRSMDPGYPTSIASVFPGINCRIDAVFQ-QDS 433
Cdd:cd00094    80 NLEPGYPKPISDLGFPPTVKQIDAALRWpdNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLDG 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2309512006 434 FFLFFSGPQYFAFNLVSR--RVTRVARSN-LWLNC 465
Cdd:cd00094   160 YYYFFKGDQYWRFDPRSKevRVGYPLKISsDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 105-264 9.99e-30

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: 112.83  E-value: 9.99e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309512006  105 GSPKWTHTNLTYRIinHTPQMSKaEVKTEIEKAFKIWSVPSTLTFTEtLEGEADINIAFVSRDHGdnsPFdgpngiLAHA 184
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVE-RTGTADIYISFGSGDSG---CT------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309512006  185 FQPGrgigGDAHFDsEETWTQDSNnynlflVAAHEFGHSLGLSHSTDPGA---LMYPNYAYREPSTYSLPQDDINGIQTI 261
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136


                   ...
gi 2309512006  262 YGP 264
Cdd:smart00235 137 YGS 139
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 378-423 1.34e-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: 59.18  E-value: 1.34e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2309512006  378 IDAAVSY-NGKTYFFVNNQCWRYDNQRrsMDPGYPTSIASVFPGINC 423
Cdd:smart00120   1 IDAAFELrDGKTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGLPC 45
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 32-87 6.13e-09

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: 51.75  E-value: 6.13e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2309512006  32 NMKTAENYLRKFYHLPSNQfrSARNATMIAEKLKEMQRFFGLPETGKPDAATIEIM 87
Cdd:pfam01471   4 DVKELQRYLNRLGYYPGPV--DGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 378-423 1.02e-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: 51.03  E-value: 1.02e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2309512006 378 IDAAVSY-NGKTYFFVNNQCWRYDNQRrsMDPGYPTSIASvFPGINC 423
Cdd:pfam00045   1 IDAAFEDrDGKTYFFKGRKYWRFDPQR--VEPGYPKLISD-FPGLPC 44
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
209-238 7.03e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 40.33  E-value: 7.03e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2309512006 209 NYNLFL-----VAAHEFGHSLGLSHSTDPGALMYP 238
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 ...
 108-263 3.57e-87

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: 263.32  E-value: 3.57e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309512006 108 KWTHTNLTYRIINHTPQMSKAEVKTEIEKAFKIWSVPSTLTFTETLEGEADINIAFVSRDHGDNSPFDGPNGILAHAFQP 187
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2309512006 188 GRGIGGDAHFDSEETWTQDSNN---YNLFLVAAHEFGHSLGLSHSTDPGALMYPNYAYREPSTYSLPQDDINGIQTIYG 263
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDPphgINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 108-263 2.35e-76

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: 235.56  E-value: 2.35e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309512006 108 KWTHTNLTYRIINHTPQMSKAEVKTEIEKAFKIWSVPSTLTFTETLEG-EADINIAFVSRDHGDNSPFDGPNGILAHAFQ 186
Cdd:cd04278     1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2309512006 187 PGrGIGGDAHFDSEETWT--QDSNNYNLFLVAAHEFGHSLGLSHSTDPGALMYPNYAYREPStYSLPQDDINGIQTIYG 263
Cdd:cd04278    81 PG-GIGGDIHFDDDEQWTlgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVPK-FKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 277-465 3.15e-75

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: 234.13  E-value: 3.15e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309512006 277 PTACDPhLRFDAATTLRGEIYFFKDKYFWRRHPQLRTVDLNFISLFWPFLPNGLQAAYEDFDRDLVFLFKGRQYWALSAY 356
Cdd:cd00094     1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309512006 357 DLQQGYPRDISNYGFPRSVQAIDAAVSY--NGKTYFFVNNQCWRYDNQRRSMDPGYPTSIASVFPGINCRIDAVFQ-QDS 433
Cdd:cd00094    80 NLEPGYPKPISDLGFPPTVKQIDAALRWpdNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLDG 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2309512006 434 FFLFFSGPQYFAFNLVSR--RVTRVARSN-LWLNC 465
Cdd:cd00094   160 YYYFFKGDQYWRFDPRSKevRVGYPLKISsDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 105-264 9.99e-30

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: 112.83  E-value: 9.99e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309512006  105 GSPKWTHTNLTYRIinHTPQMSKaEVKTEIEKAFKIWSVPSTLTFTEtLEGEADINIAFVSRDHGdnsPFdgpngiLAHA 184
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSP-EEREAIAKALAEWSDVTCIRFVE-RTGTADIYISFGSGDSG---CT------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309512006  185 FQPGrgigGDAHFDsEETWTQDSNnynlflVAAHEFGHSLGLSHSTDPGA---LMYPNYAYREPSTYSLPQDDINGIQTI 261
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136


                   ...
gi 2309512006  262 YGP 264
Cdd:smart00235 137 YGS 139
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 134-263 8.13e-16

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: 74.80  E-value: 8.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309512006 134 IEKAFKIWS--VPSTLTFTETLEGEADINIAFVSRDHGDNSPfdgpnGILAHAFQPGRGIGGDAHFDSEE---TWTQDSN 208
Cdd:cd04279    26 VKQAAAEWEnvGPLKFVYNPEEDNDADIVIFFDRPPPVGGAG-----GGLARAGFPLISDGNRKLFNRTDinlGPGQPRG 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2309512006 209 NYNLFLVAAHEFGHSLGLSHSTD-PGALMYPNYAYREPSTYSLPQDDINGIQTIYG 263
Cdd:cd04279   101 AENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 128-263 2.32e-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: 2.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309512006 128 AEVKTEIEKAFKIWSVPSTLTFTETLEGE-ADINIAFVSRDHGDNspfdgpngiLAHAFQPGRGI----GGDAHFDSEET 202
Cdd:cd04277    33 AAQQAAARDALEAWEDVADIDFVEVSDNSgADIRFGNSSDPDGNT---------AGYAYYPGSGSgtayGGDIWFNSSYD 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309512006 203 WTQDS-NNYNlFLVAAHEFGHSLGLSHSTDPGA----------------LM--------YPNYAYREPSTYSLpqDDING 257
Cdd:cd04277   104 TNSDSpGSYG-YQTIIHEIGHALGLEHPGDYNGgdpvpptyaldsreytVMsynsgygnGASAGGGYPQTPML--LDIAA 180


                  ....*.
gi 2309512006 258 IQTIYG 263
Cdd:cd04277   181 LQYLYG 186
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 378-423 1.34e-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: 59.18  E-value: 1.34e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2309512006  378 IDAAVSY-NGKTYFFVNNQCWRYDNQRrsMDPGYPTSIASVFPGINC 423
Cdd:smart00120   1 IDAAFELrDGKTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGLPC 45
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 126-262 3.47e-11

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: 61.77  E-value: 3.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309512006 126 SKAEVKTEIEKAFKIWSVPSTLTFTETLEGEADINIAFVsrdhgdNSPFDGPNGILAHAFqpgrgIGGDAHFDSEETWTQ 205
Cdd:cd00203    19 LSAQIQSLILIAMQIWRDYLNIRFVLVGVEIDKADIAIL------VTRQDFDGGTGGWAY-----LGRVCDSLRGVGVLQ 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309512006 206 D--SNNYNLFLVAAHEFGHSLGLSHS--------------------TDPGALMYPnYAYREPSTYSLP--QDDINGIQTI 261
Cdd:cd00203    88 DnqSGTKEGAQTIAHELGHALGFYHDhdrkdrddyptiddtlnaedDDYYSVMSY-TKGSFSDGQRKDfsQCDIDQINKL 166


                  .
gi 2309512006 262 Y 262
Cdd:cd00203   167 Y 167
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 32-87 6.13e-09

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: 51.75  E-value: 6.13e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2309512006  32 NMKTAENYLRKFYHLPSNQfrSARNATMIAEKLKEMQRFFGLPETGKPDAATIEIM 87
Cdd:pfam01471   4 DVKELQRYLNRLGYYPGPV--DGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 378-423 1.02e-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: 51.03  E-value: 1.02e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2309512006 378 IDAAVSY-NGKTYFFVNNQCWRYDNQRrsMDPGYPTSIASvFPGINC 423
Cdd:pfam00045   1 IDAAFEDrDGKTYFFKGRKYWRFDPQR--VEPGYPKLISD-FPGLPC 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 286-327 9.31e-08

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 48.39  E-value: 9.31e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2309512006  286 FDAATTLR-GEIYFFKDKYFWRRHPQ-LRTVDLNFISLFWPFLP 327
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKrVDPGYPKLISSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 330-372 6.24e-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: 46.02  E-value: 6.24e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2309512006 330 LQAAYEDfDRDLVFLFKGRQYWALSAYDLQQGYPRDISNY-GFP 372
Cdd:pfam00045   1 IDAAFED-RDGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLP 43
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 114-262 1.27e-06

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


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 48.26  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309512006 114 LTYRIINHTPQMSKAEVK---TEIEKAFKIwsvpstlTFTETLEG-EADINIAFVSrdhgDNSPFDGPNGILAHAFQPGR 189
Cdd:cd04268     4 ITYYIDDSVPDKLRAAILdaiEAWNKAFAI-------GFKNANDVdPADIRYSVIR----WIPYNDGTWSYGPSQVDPLT 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309512006 190 GIGGDAHFDSEETWTQDSNNYnLFLVAAHEFGHSLGLSHS----------------TDPGALMYP---NYAYREP--STY 248
Cdd:cd04268    73 GEILLARVYLYSSFVEYSGAR-LRNTAEHELGHALGLRHNfaasdrddnvdllaekGDTSSVMDYapsNFSIQLGdgQKY 151

                         170
                  ....*....|....
gi 2309512006 249 SLPQDDINGIQTIY 262
Cdd:cd04268   152 TIGPYDIAAIKKLY 165
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 330-373 7.47e-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: 43.00  E-value: 7.47e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2309512006  330 LQAAYEDfDRDLVFLFKGRQYWALSAYDLQQGYPRDISNY--GFPR 373
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFfpGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 286-328 3.70e-05

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: 41.01  E-value: 3.70e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2309512006 286 FDAATTLR-GEIYFFKDKYFWRRHPQ-LRTVDLNFISLFwPFLPN 328
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQrVEPGYPKLISDF-PGLPC 44
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 128-228 8.28e-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: 43.52  E-value: 8.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309512006 128 AEVKTEIEKAFKIWSVPSTLTFTETLEGEADINIAFvsRDHGDNSPFDGPNGILAHAFQPGRGiggdahFDSEETWTQDS 207
Cdd:cd04327    19 AFLKDKVRAAAREWLPYANLKFKFVTDADADIRISF--TPGDGYWSYVGTDALLIGADAPTMN------LGWFTDDTPDP 90

                          90       100
                  ....*....|....*....|.
gi 2309512006 208 NNYNlflVAAHEFGHSLGLSH 228
Cdd:cd04327    91 EFSR---VVLHEFGHALGFIH 108
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
209-238 7.03e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 40.33  E-value: 7.03e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2309512006 209 NYNLFL-----VAAHEFGHSLGLSHSTDPGALMYP 238
Cdd:COG1913   115 DEELFLervlkEAVHELGHLFGLGHCPNPRCVMHF 149
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
147-265 2.04e-03

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 39.32  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2309512006 147 LTFTETLEGEADINIAFVSRDhgdnspFDGPNGILAHAFQP-GRGIGGDAHFDSEETwTQDSNNYNLFLVAAHEFGHSLG 225
Cdd:pfam13688  78 FQDFSAWRGTQNDDLAYLFLM------TNCSGGGLAWLGQLcNSGSAGSVSTRVSGN-NVVVSTATEWQVFAHEIGHNFG 150

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2309512006 226 LSHstDPGAlmYPNYAYREPSTYSLPqddiNGIQTIYGPS 265
Cdd:pfam13688 151 AVH--DCDS--STSSQCCPPSNSTCP----AGGRYIMNPS 182
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 209-238 9.93e-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: 36.89  E-value: 9.93e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2309512006 209 NYNLFL-----VAAHEFGHSLGLSHSTDPGALMYP 238
Cdd:cd11375   115 DEGLFLerllkEAVHELGHLFGLDHCPYYACVMNF 149
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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