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Conserved domains on  [gi|180618|gb|AAA88021|]
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neutrophil collagenase [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 ...
 107-262 7.34e-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: 7.34e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 180618     107 KWERTNLTYRIRNYTPQLSEAEVERAIKDAFELWSVASPLIFTRISQGEADINIAFYQRDHGDNSPFDGPNGILAHAFQP 186
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 180618     187 GQGIGGDAHFDAEETWT---NTSANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFRETSNYSLPQDDIDGIQAIYG 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 2.88e-77

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: 239.52  E-value: 2.88e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 180618   276 PKPCDPsLTFDAITTLRGEILFFKDRYFWRRHPQLQRVEMNFISLFWPSLPTGIQAAYEDFDRDLIFLFKGNQYWALSGY 355
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 180618   356 DILQGYPKDISNYGFPSSVQAIDAAVFY--RSKTYFFVNDQFWRYDNQRQFMEPGYPKSISGAFPGIESKVDAVFQ-QEH 432
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWpdNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 180618   433 FFHVFSGPRYYAFDLIAQ--RVTRVARGNK-WLNC 464
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSKevRVGYPLKISSdWLGC 194
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 29-86 3.25e-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: 52.52  E-value: 3.25e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 180618      29 NTKTVQDYLEKFYQLPSNQyqsTRKNGTNViVEKLKEMQRFFGLNVTGKPNEETLDMM 86
Cdd:pfam01471   4 DVKELQRYLNRLGYYPGPV---DGYFGPST-EAAVKAFQRAFGLPVDGIVDPETLAAL 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 7.34e-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: 7.34e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 180618     107 KWERTNLTYRIRNYTPQLSEAEVERAIKDAFELWSVASPLIFTRISQGEADINIAFYQRDHGDNSPFDGPNGILAHAFQP 186
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 180618     187 GQGIGGDAHFDAEETWT---NTSANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFRETSNYSLPQDDIDGIQAIYG 262
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTvgsDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 107-262 1.04e-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: 244.42  E-value: 1.04e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 180618   107 KWERTNLTYRIRNYTPQLSEAEVERAIKDAFELWSVASPLIFTRI-SQGEADINIAFYQRDHGDNSPFDGPNGILAHAFQ 185
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 180618   186 PGqGIGGDAHFDAEETWT--NTSANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFREtSNYSLPQDDIDGIQAIYG 262
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTlgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV-PKFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 276-464 2.88e-77

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: 239.52  E-value: 2.88e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 180618   276 PKPCDPsLTFDAITTLRGEILFFKDRYFWRRHPQLQRVEMNFISLFWPSLPTGIQAAYEDFDRDLIFLFKGNQYWALSGY 355
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 180618   356 DILQGYPKDISNYGFPSSVQAIDAAVFY--RSKTYFFVNDQFWRYDNQRQFMEPGYPKSISGAFPGIESKVDAVFQ-QEH 432
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWpdNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 180618   433 FFHVFSGPRYYAFDLIAQ--RVTRVARGNK-WLNC 464
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSKevRVGYPLKISSdWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 104-262 1.48e-31

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: 117.84  E-value: 1.48e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 180618      104 GNPKWERTNLTYRIrnYTPQLSEAEVErAIKDAFELWSVASPLIFTRISQGeADINIAFYQRDHGdnsPFdgpngiLAHA 183
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPEERE-AIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDSG---CT------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 180618      184 FQPGqgigGDAHFDaEETWTNTSAnynlflVAAHEFGHSLGLAHSSDPGA---LMYPNYAFRETSNYSLPQDDIDGIQAI 260
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136


                   ..
gi 180618      261 YG 262
Cdd:smart00235 137 YG 138
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 377-422 3.70e-10

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: 54.94  E-value: 3.70e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 180618      377 IDAAVFYR-SKTYFFVNDQFWRYDNQRqfMEPGYPKSISGAFPGIES 422
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 377-422 3.18e-09

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: 52.18  E-value: 3.18e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 180618     377 IDAAVFYRS-KTYFFVNDQFWRYDNQRqfMEPGYPKSISGaFPGIES 422
Cdd:pfam00045   1 IDAAFEDRDgKTYFFKGRKYWRFDPQR--VEPGYPKLISD-FPGLPC 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 29-86 3.25e-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: 52.52  E-value: 3.25e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 180618      29 NTKTVQDYLEKFYQLPSNQyqsTRKNGTNViVEKLKEMQRFFGLNVTGKPNEETLDMM 86
Cdd:pfam01471   4 DVKELQRYLNRLGYYPGPV---DGYFGPST-EAAVKAFQRAFGLPVDGIVDPETLAAL 57
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 132-271 8.63e-06

Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 46.99  E-value: 8.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 180618   132 AIKDAFELWSVASPLifTRISQGE-ADINIAFyqRDHGDNSPFDGPNGI-LAHA-FQPGQGIGGDAHFDAEETWTNTSAN 208
Cdd:COG5549 105 AVLQAIAEWNAYLPL--EVVENPEnADIIIVR--SNPPLTASPNPETGArSAETtYEFYDTGNILSHRFTILLSPNQTGK 180

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 180618   209 YnlfLVAA--HEFGHSLGL-AHSSDPGALMYpnyaFRETSN-YSLPQDDIDGIQAIYGlssnpiQPT 271
Cdd:COG5549 181 Y---LLATarHELGHALGIwGHSPSPTDAMY----FSQVRNpPPISPRDINTLKRIYQ------QPT 234
 
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 7.34e-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: 7.34e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 180618     107 KWERTNLTYRIRNYTPQLSEAEVERAIKDAFELWSVASPLIFTRISQGEADINIAFYQRDHGDNSPFDGPNGILAHAFQP 186
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 180618     187 GQGIGGDAHFDAEETWT---NTSANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFRETSNYSLPQDDIDGIQAIYG 262
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTvgsDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 107-262 1.04e-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: 244.42  E-value: 1.04e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 180618   107 KWERTNLTYRIRNYTPQLSEAEVERAIKDAFELWSVASPLIFTRI-SQGEADINIAFYQRDHGDNSPFDGPNGILAHAFQ 185
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 180618   186 PGqGIGGDAHFDAEETWT--NTSANYNLFLVAAHEFGHSLGLAHSSDPGALMYPNYAFREtSNYSLPQDDIDGIQAIYG 262
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTlgSDSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV-PKFKLSQDDIRGIQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 276-464 2.88e-77

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: 239.52  E-value: 2.88e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 180618   276 PKPCDPsLTFDAITTLRGEILFFKDRYFWRRHPQLQRVEMNFISLFWPSLPTGIQAAYEDFDRDLIFLFKGNQYWALSGY 355
Cdd:cd00094   1 PDACDP-LSFDAVTTLRGELYFFKGRYFWRLSPGKPPGSPFLISSFWPSLPSPVDAAFERPDTGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 180618   356 DILQGYPKDISNYGFPSSVQAIDAAVFY--RSKTYFFVNDQFWRYDNQRQFMEPGYPKSISGAFPGIESKVDAVFQ-QEH 432
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWpdNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIETDFPGVPDKVDAAFRwLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 180618   433 FFHVFSGPRYYAFDLIAQ--RVTRVARGNK-WLNC 464
Cdd:cd00094 160 YYYFFKGDQYWRFDPRSKevRVGYPLKISSdWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 104-262 1.48e-31

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: 117.84  E-value: 1.48e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 180618      104 GNPKWERTNLTYRIrnYTPQLSEAEVErAIKDAFELWSVASPLIFTRISQGeADINIAFYQRDHGdnsPFdgpngiLAHA 183
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPEERE-AIAKALAEWSDVTCIRFVERTGT-ADIYISFGSGDSG---CT------LSHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 180618      184 FQPGqgigGDAHFDaEETWTNTSAnynlflVAAHEFGHSLGLAHSSDPGA---LMYPNYAFRETSNYSLPQDDIDGIQAI 260
Cdd:smart00235  68 GRPG----GDQHLS-LGNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSEDDSLGIPYD 136


                   ..
gi 180618      261 YG 262
Cdd:smart00235 137 YG 138
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 132-262 2.47e-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: 75.96  E-value: 2.47e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 180618   132 AIKDAFELWSVASPLIFTRISQGEADINIAFYQRDhgdNSPFDGPNGILAHAFQPGQGIGGDA---HFDAEETWTNTSAN 208
Cdd:cd04279  25 AVKQAAAEWENVGPLKFVYNPEEDNDADIVIFFDR---PPPVGGAGGGLARAGFPLISDGNRKlfnRTDINLGPGQPRGA 101

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 180618   209 YNLFLVAAHEFGHSLGLAHSSD-PGALMYPNYAFRETSNYSLPQDDIDGIQAIYG 262
Cdd:cd04279 102 ENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 120-262 4.34e-14

Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 70.52  E-value: 4.34e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 180618   120 YTPQLSEAEVErAIKDAFELWSVASPLIFTRISQGE-ADINIAFYQRDHGDNspfdgpngiLAHAFQPG----QGIGGDA 194
Cdd:cd04277  27 NTAALSAAQQA-AARDALEAWEDVADIDFVEVSDNSgADIRFGNSSDPDGNT---------AGYAYYPGsgsgTAYGGDI 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 180618   195 HFDAEETWTNTSA-NYNlFLVAAHEFGHSLGLAHSSDPGAL-MYPNYAFRETSNYSL-----------------PQ---- 251
Cdd:cd04277  97 WFNSSYDTNSDSPgSYG-YQTIIHEIGHALGLEHPGDYNGGdPVPPTYALDSREYTVmsynsgygngasagggyPQtpml 175

                       170
                ....*....|.
gi 180618   252 DDIDGIQAIYG 262
Cdd:cd04277 176 LDIAALQYLYG 186
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 377-422 3.70e-10

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: 54.94  E-value: 3.70e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 180618      377 IDAAVFYR-SKTYFFVNDQFWRYDNQRqfMEPGYPKSISGAFPGIES 422
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKR--VDPGYPKLISSFFPGLPC 45
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 118-261 4.49e-10

Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 58.30  E-value: 4.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 180618   118 RNYTPQLSEAEVERAIKDAFELWSVASPLIFTRISQGE--ADINIAFYQRDHgdnspfdgPNGILAHAFQPG--QGIGGD 193
Cdd:cd00203  12 RDVEEENLSAQIQSLILIAMQIWRDYLNIRFVLVGVEIdkADIAILVTRQDF--------DGGTGGWAYLGRvcDSLRGV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 180618   194 AHFDaeetwTNTSANYNLFLVAAHEFGHSLGLAHSSD--------------------PGALMYP-NYAFRETSNYSLPQD 252
Cdd:cd00203  84 GVLQ-----DNQSGTKEGAQTIAHELGHALGFYHDHDrkdrddyptiddtlnaedddYYSVMSYtKGSFSDGQRKDFSQC 158


                ....*....
gi 180618   253 DIDGIQAIY 261
Cdd:cd00203 159 DIDQINKLY 167
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 377-422 3.18e-09

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: 52.18  E-value: 3.18e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 180618     377 IDAAVFYRS-KTYFFVNDQFWRYDNQRqfMEPGYPKSISGaFPGIES 422
Cdd:pfam00045   1 IDAAFEDRDgKTYFFKGRKYWRFDPQR--VEPGYPKLISD-FPGLPC 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 29-86 3.25e-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: 52.52  E-value: 3.25e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 180618      29 NTKTVQDYLEKFYQLPSNQyqsTRKNGTNViVEKLKEMQRFFGLNVTGKPNEETLDMM 86
Cdd:pfam01471   4 DVKELQRYLNRLGYYPGPV---DGYFGPST-EAAVKAFQRAFGLPVDGIVDPETLAAL 57
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 113-261 1.50e-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: 54.04  E-value: 1.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 180618   113 LTYRIRNYTPQlseaEVERAIKDAFELWSVASPLIFT-RISQGEADINIAFYQrdhgDNSPFDGPNGILAHAFQPGQGIG 191
Cdd:cd04268   4 ITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKnANDVDPADIRYSVIR----WIPYNDGTWSYGPSQVDPLTGEI 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 180618   192 GDAHFDAEETWTNTSANYnLFLVAAHEFGHSLGLAHSS----------------DPGALMYP-----NYAFRETSNYSLP 250
Cdd:cd04268  76 LLARVYLYSSFVEYSGAR-LRNTAEHELGHALGLRHNFaasdrddnvdllaekgDTSSVMDYapsnfSIQLGDGQKYTIG 154

                       170
                ....*....|.
gi 180618   251 QDDIDGIQAIY 261
Cdd:cd04268 155 PYDIAAIKKLY 165
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 329-372 1.01e-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: 47.95  E-value: 1.01e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 180618     329 IQAAYEDfDRDLIFLFKGNQYWALSGYDILQGYPKDISNY-GFPS 372
Cdd:pfam00045   1 IDAAFED-RDGKTYFFKGRKYWRFDPQRVEPGYPKLISDFpGLPC 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 329-372 6.19e-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: 6.19e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 180618      329 IQAAYEDfDRDLIFLFKGNQYWALSGYDILQGYPKDISNY--GFPS 372
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFfpGLPC 45
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 285-326 1.07e-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: 45.31  E-value: 1.07e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 180618      285 FDAITTLR-GEILFFKDRYFWRRHPQ-LQRVEMNFISLFWPSLP 326
Cdd:smart00120   1 IDAAFELRdGKTYFFKGDKYWRFDPKrVDPGYPKLISSFFPGLP 44
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 132-271 8.63e-06

Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 46.99  E-value: 8.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 180618   132 AIKDAFELWSVASPLifTRISQGE-ADINIAFyqRDHGDNSPFDGPNGI-LAHA-FQPGQGIGGDAHFDAEETWTNTSAN 208
Cdd:COG5549 105 AVLQAIAEWNAYLPL--EVVENPEnADIIIVR--SNPPLTASPNPETGArSAETtYEFYDTGNILSHRFTILLSPNQTGK 180

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 180618   209 YnlfLVAA--HEFGHSLGL-AHSSDPGALMYpnyaFRETSN-YSLPQDDIDGIQAIYGlssnpiQPT 271
Cdd:COG5549 181 Y---LLATarHELGHALGIwGHSPSPTDAMY----FSQVRNpPPISPRDINTLKRIYQ------QPT 234
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 285-326 5.95e-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: 40.24  E-value: 5.95e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 180618     285 FDAITTLR-GEILFFKDRYFWRRHPQ-LQRVEMNFISLFwPSLP 326
Cdd:pfam00045   1 IDAAFEDRdGKTYFFKGRKYWRFDPQrVEPGYPKLISDF-PGLP 43
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 125-227 8.94e-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: 8.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 180618   125 SEAEVERAIKDAFELWSVASPLIFTRISQGEADINIAFYqRDHGDNSpFDGPNGILAHAFQPGQGIGGDAHFDAEETWTN 204
Cdd:cd04327  17 PDAFLKDKVRAAAREWLPYANLKFKFVTDADADIRISFT-PGDGYWS-YVGTDALLIGADAPTMNLGWFTDDTPDPEFSR 94

                        90       100
                ....*....|....*....|...
gi 180618   205 TsanynlflvAAHEFGHSLGLAH 227
Cdd:cd04327  95 V---------VLHEFGHALGFIH 108
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
206-237 1.05e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 39.94  E-value: 1.05e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 180618   206 SANYNLFL-----VAAHEFGHSLGLAHSSDPGALMYP 237
Cdd:COG1913 113 PPDEELFLervlkEAVHELGHLFGLGHCPNPRCVMHF 149
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
 154-227 2.74e-03

Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma protein A (PAPP-A or pappalysin-1) cleaves insulin-like growth factor-binding proteins 4 and 5, thereby promoting cell growth by releasing bound growth factor. This model includes pappalysins and related metalloprotease domains from all three kingdoms of life. The three-dimensional structure of an archaeal representative, ulilysin, has been solved.


Pssm-ID: 239802 [Multi-domain]  Cd Length: 225  Bit Score: 39.25  E-value: 2.74e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 180618   154 GEADINIAFYQrdhgdnspfDGPNGILAHAFQPGQGIGGDAHFD-----AEETWTNTSANYNLFLVAAHEFGHSLGLAH 227
Cdd:cd04275  84 GYKYLNIYVAN---------FLGGGLLGYATFPDSLVSLAFITDgvvinPSSLPGGSAAPYNLGDTATHEVGHWLGLYH 153
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 207-253 6.67e-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: 37.66  E-value: 6.67e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 180618   207 ANYNLFL-----VAAHEFGHSLGLAHSSDPGALMYPnyafretSNySLPQDD 253
Cdd:cd11375 114 PDEGLFLerllkEAVHELGHLFGLDHCPYYACVMNF-------SN-SLEETD 157
 
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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